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human magi1 gene  (OriGene)


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    Structured Review

    OriGene human magi1 gene
    (A) The neighbor-joining (NJ) tree dendrogram of the WW domains from human origin. The WW domain sequences from human origin were obtained from the Pfam server (http://www.sanger.ac.uk/Software/Pfam/), and the redundancy was removed using the 100% sequence identity filter. The sequences thus selected were analyzed using the program CLUSTAL W (Thompson et al. 1994). (Magenta) The members of the subclass that contains SAV1 WW2 and <t>MAGI1</t> WW2. (B) Comparative representation of the LOGO plot of the representative WW domain sequences and the sequences of the members of the subclass that contains SAV1 WW2 and MAG1 WW2. (Yellow boxes) Polar residues of E242 and S246 in SAV1 WW2, as well as those of their counterparts in MAGI1 WW2, E366 and D370. (Red) Acidic residues, (blue) basic residues.
    Human Magi1 Gene, supplied by OriGene, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+magi1+gene/pmc02525516-218-5-22?v=OriGene
    Average 90 stars, based on 1 article reviews
    human magi1 gene - by Bioz Stars, 2026-08
    90/100 stars

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    1) Product Images from "Structural basis for controlling the dimerization and stability of the WW domains of an atypical subfamily"

    Article Title: Structural basis for controlling the dimerization and stability of the WW domains of an atypical subfamily

    Journal:

    doi: 10.1110/ps.035329.108

    (A) The neighbor-joining (NJ) tree dendrogram of the WW domains from human origin. The WW domain sequences from human origin were obtained from the Pfam server (http://www.sanger.ac.uk/Software/Pfam/), and the redundancy was removed using the 100% sequence identity filter. The sequences thus selected were analyzed using the program CLUSTAL W (Thompson et al. 1994). (Magenta) The members of the subclass that contains SAV1 WW2 and MAGI1 WW2. (B) Comparative representation of the LOGO plot of the representative WW domain sequences and the sequences of the members of the subclass that contains SAV1 WW2 and MAG1 WW2. (Yellow boxes) Polar residues of E242 and S246 in SAV1 WW2, as well as those of their counterparts in MAGI1 WW2, E366 and D370. (Red) Acidic residues, (blue) basic residues.
    Figure Legend Snippet: (A) The neighbor-joining (NJ) tree dendrogram of the WW domains from human origin. The WW domain sequences from human origin were obtained from the Pfam server (http://www.sanger.ac.uk/Software/Pfam/), and the redundancy was removed using the 100% sequence identity filter. The sequences thus selected were analyzed using the program CLUSTAL W (Thompson et al. 1994). (Magenta) The members of the subclass that contains SAV1 WW2 and MAGI1 WW2. (B) Comparative representation of the LOGO plot of the representative WW domain sequences and the sequences of the members of the subclass that contains SAV1 WW2 and MAG1 WW2. (Yellow boxes) Polar residues of E242 and S246 in SAV1 WW2, as well as those of their counterparts in MAGI1 WW2, E366 and D370. (Red) Acidic residues, (blue) basic residues.

    Techniques Used: Software, Sequencing

    Equilibrium analytical ultracentrifugation of MAGI1 WW2 355–390. (Bottom panel) Radial distribution of the absorbance in the centrifuge cell at equilibrium at 16,000 rpm, with a protein concentration of 0.5 mg/mL. The solid line through the data represents the fit to a single species with a molecular weight corresponding to 5611, while the theoretical molecular weight for the single polypeptide chain is 5580. (Upper panels) Residuals for the fit.
    Figure Legend Snippet: Equilibrium analytical ultracentrifugation of MAGI1 WW2 355–390. (Bottom panel) Radial distribution of the absorbance in the centrifuge cell at equilibrium at 16,000 rpm, with a protein concentration of 0.5 mg/mL. The solid line through the data represents the fit to a single species with a molecular weight corresponding to 5611, while the theoretical molecular weight for the single polypeptide chain is 5580. (Upper panels) Residuals for the fit.

    Techniques Used: Protein Concentration, Molecular Weight

    (A) The 1H-15N HSQC spectrum of MAGI1 WW2 355–390, with labels. (*) Signals from the N- and C-terminal artificial tags of the present construct. (B) Solution structures of MAGI1 WW2 355–390, in line representations. (Cyan) Residues in the N- and C-terminal artificial tags of the present construct.
    Figure Legend Snippet: (A) The 1H-15N HSQC spectrum of MAGI1 WW2 355–390, with labels. (*) Signals from the N- and C-terminal artificial tags of the present construct. (B) Solution structures of MAGI1 WW2 355–390, in line representations. (Cyan) Residues in the N- and C-terminal artificial tags of the present construct.

    Techniques Used: Construct

    Structural comparison between mSAV1 WW2 231–266 and hMAGI1 WW2 355–390. (A) Structure of SAV1 WW2 231–266. (Lines) Side chains of key aromatic residues (F249, Y252, H256, Y263) buried in the interface of the homodimer; (neon bars) side chains of the polar residues (E242, S246). These side chains are colored to clarify the representation of the molecular interaction. (B) Structure of MAGI1 WW2 355–390. (Lines) Side chains of the aromatic residues (Y373, Y376, H380, Y387); (neon bars) side chains of the polar residues (E366, D370).
    Figure Legend Snippet: Structural comparison between mSAV1 WW2 231–266 and hMAGI1 WW2 355–390. (A) Structure of SAV1 WW2 231–266. (Lines) Side chains of key aromatic residues (F249, Y252, H256, Y263) buried in the interface of the homodimer; (neon bars) side chains of the polar residues (E242, S246). These side chains are colored to clarify the representation of the molecular interaction. (B) Structure of MAGI1 WW2 355–390. (Lines) Side chains of the aromatic residues (Y373, Y376, H380, Y387); (neon bars) side chains of the polar residues (E366, D370).

    Techniques Used:

    (A) The 1H-15N HSQC spectrum of MAGI1 WW2 355–401, with labels. (*) Signals from the N- and C-terminal artificial tags of the present construct. (B) Solution structures of MAGI1 WW2 355–401, in line representations. (Cyan) Residues in the N- and C-terminal artificial tags of the present construct.
    Figure Legend Snippet: (A) The 1H-15N HSQC spectrum of MAGI1 WW2 355–401, with labels. (*) Signals from the N- and C-terminal artificial tags of the present construct. (B) Solution structures of MAGI1 WW2 355–401, in line representations. (Cyan) Residues in the N- and C-terminal artificial tags of the present construct.

    Techniques Used: Construct

    The 15N spin relaxation profiles of MAGI1 WW2 355–390 (black), MAGI1 WW2 355–401 (red), and MAGI1 WW2 355–390 D370S (green). The heteronuclear NOE (top), longitudinal (R1; middle), and transverse (R2; bottom) relaxation profiles are shown with error bars. (Cyan arrows) β-strands, (red bar) the α-helix of the longer construct, MAGI1 WW2 355–401.
    Figure Legend Snippet: The 15N spin relaxation profiles of MAGI1 WW2 355–390 (black), MAGI1 WW2 355–401 (red), and MAGI1 WW2 355–390 D370S (green). The heteronuclear NOE (top), longitudinal (R1; middle), and transverse (R2; bottom) relaxation profiles are shown with error bars. (Cyan arrows) β-strands, (red bar) the α-helix of the longer construct, MAGI1 WW2 355–401.

    Techniques Used: Construct

    Thermal stability summary of MAGI1 WW2 355–390 and its variants
    Figure Legend Snippet: Thermal stability summary of MAGI1 WW2 355–390 and its variants

    Techniques Used:

    (A) Far-UV CD spectra of MAGI1 WW2 355–390 (black), MAGI1 WW2 355–401 (red), and MAGI1 WW2 355–390 D370S (green), recorded at 20°C. (B) Thermal denaturation profiles of MAGI1 WW2 355–390 (black), MAGI1 WW2 355–401 (red), and those of the D370S mutant, recorded with 55 μM (green) and 5 μM (blue) protein concentrations. The changes in ellipticity at 232 nm for MAGI1 WW2 355–390 and MAGI1 WW2 355–390 D370S, and that at 217 nm for MAGI1 WW2 355–401, were monitored and analyzed as a function of temperature.
    Figure Legend Snippet: (A) Far-UV CD spectra of MAGI1 WW2 355–390 (black), MAGI1 WW2 355–401 (red), and MAGI1 WW2 355–390 D370S (green), recorded at 20°C. (B) Thermal denaturation profiles of MAGI1 WW2 355–390 (black), MAGI1 WW2 355–401 (red), and those of the D370S mutant, recorded with 55 μM (green) and 5 μM (blue) protein concentrations. The changes in ellipticity at 232 nm for MAGI1 WW2 355–390 and MAGI1 WW2 355–390 D370S, and that at 217 nm for MAGI1 WW2 355–401, were monitored and analyzed as a function of temperature.

    Techniques Used: Mutagenesis

    (A) Close-up view highlighting the interactions around the C-terminal α-helix in MAGI1 WW2 355–401. Key residues described in the main text are marked. (B) Structural comparison between MAGI1 WW2 355–390 (blue) and MAGI1 WW2 355–401 (red). Structures were superimposed using the backbone heavy atoms in the region between Leu361 and Pro390. (C) Comparison of the accessible surface areas of the residues between MAGI1 WW2 355–390 (black) and MAGI1 WW2 355–401 (red). (Cyan bars) β-strands; (red bar) the α-helix of the longer construct, MAGI1 WW2 355–401.
    Figure Legend Snippet: (A) Close-up view highlighting the interactions around the C-terminal α-helix in MAGI1 WW2 355–401. Key residues described in the main text are marked. (B) Structural comparison between MAGI1 WW2 355–390 (blue) and MAGI1 WW2 355–401 (red). Structures were superimposed using the backbone heavy atoms in the region between Leu361 and Pro390. (C) Comparison of the accessible surface areas of the residues between MAGI1 WW2 355–390 (black) and MAGI1 WW2 355–401 (red). (Cyan bars) β-strands; (red bar) the α-helix of the longer construct, MAGI1 WW2 355–401.

    Techniques Used: Construct



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    (A) The neighbor-joining (NJ) tree dendrogram of the WW domains from human origin. The WW domain sequences from human origin were obtained from the Pfam server (http://www.sanger.ac.uk/Software/Pfam/), and the redundancy was removed using the 100% sequence identity filter. The sequences thus selected were analyzed using the program CLUSTAL W (Thompson et al. 1994). (Magenta) The members of the subclass that contains SAV1 WW2 and <t>MAGI1</t> WW2. (B) Comparative representation of the LOGO plot of the representative WW domain sequences and the sequences of the members of the subclass that contains SAV1 WW2 and MAG1 WW2. (Yellow boxes) Polar residues of E242 and S246 in SAV1 WW2, as well as those of their counterparts in MAGI1 WW2, E366 and D370. (Red) Acidic residues, (blue) basic residues.
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    (A) The neighbor-joining (NJ) tree dendrogram of the WW domains from human origin. The WW domain sequences from human origin were obtained from the Pfam server (http://www.sanger.ac.uk/Software/Pfam/), and the redundancy was removed using the 100% sequence identity filter. The sequences thus selected were analyzed using the program CLUSTAL W (Thompson et al. 1994). (Magenta) The members of the subclass that contains SAV1 WW2 and <t>MAGI1</t> WW2. (B) Comparative representation of the LOGO plot of the representative WW domain sequences and the sequences of the members of the subclass that contains SAV1 WW2 and MAG1 WW2. (Yellow boxes) Polar residues of E242 and S246 in SAV1 WW2, as well as those of their counterparts in MAGI1 WW2, E366 and D370. (Red) Acidic residues, (blue) basic residues.
    Human Magi1 Gene Cdna Clone, supplied by OriGene, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    (A) The neighbor-joining (NJ) tree dendrogram of the WW domains from human origin. The WW domain sequences from human origin were obtained from the Pfam server (http://www.sanger.ac.uk/Software/Pfam/), and the redundancy was removed using the 100% sequence identity filter. The sequences thus selected were analyzed using the program CLUSTAL W (Thompson et al. 1994). (Magenta) The members of the subclass that contains SAV1 WW2 and MAGI1 WW2. (B) Comparative representation of the LOGO plot of the representative WW domain sequences and the sequences of the members of the subclass that contains SAV1 WW2 and MAG1 WW2. (Yellow boxes) Polar residues of E242 and S246 in SAV1 WW2, as well as those of their counterparts in MAGI1 WW2, E366 and D370. (Red) Acidic residues, (blue) basic residues.

    Journal:

    Article Title: Structural basis for controlling the dimerization and stability of the WW domains of an atypical subfamily

    doi: 10.1110/ps.035329.108

    Figure Lengend Snippet: (A) The neighbor-joining (NJ) tree dendrogram of the WW domains from human origin. The WW domain sequences from human origin were obtained from the Pfam server (http://www.sanger.ac.uk/Software/Pfam/), and the redundancy was removed using the 100% sequence identity filter. The sequences thus selected were analyzed using the program CLUSTAL W (Thompson et al. 1994). (Magenta) The members of the subclass that contains SAV1 WW2 and MAGI1 WW2. (B) Comparative representation of the LOGO plot of the representative WW domain sequences and the sequences of the members of the subclass that contains SAV1 WW2 and MAG1 WW2. (Yellow boxes) Polar residues of E242 and S246 in SAV1 WW2, as well as those of their counterparts in MAGI1 WW2, E366 and D370. (Red) Acidic residues, (blue) basic residues.

    Article Snippet: Plasmids The DNA encoding the human MAGI1 gene was subcloned by PCR from the human cDNA clone locus {"type":"entrez-nucleotide","attrs":{"text":"NM_004742","term_id":"66346707"}} NM_004742 (TrueClone Collection, OriGene, Cat No. SC117150).

    Techniques: Software, Sequencing

    Equilibrium analytical ultracentrifugation of MAGI1 WW2 355–390. (Bottom panel) Radial distribution of the absorbance in the centrifuge cell at equilibrium at 16,000 rpm, with a protein concentration of 0.5 mg/mL. The solid line through the data represents the fit to a single species with a molecular weight corresponding to 5611, while the theoretical molecular weight for the single polypeptide chain is 5580. (Upper panels) Residuals for the fit.

    Journal:

    Article Title: Structural basis for controlling the dimerization and stability of the WW domains of an atypical subfamily

    doi: 10.1110/ps.035329.108

    Figure Lengend Snippet: Equilibrium analytical ultracentrifugation of MAGI1 WW2 355–390. (Bottom panel) Radial distribution of the absorbance in the centrifuge cell at equilibrium at 16,000 rpm, with a protein concentration of 0.5 mg/mL. The solid line through the data represents the fit to a single species with a molecular weight corresponding to 5611, while the theoretical molecular weight for the single polypeptide chain is 5580. (Upper panels) Residuals for the fit.

    Article Snippet: Plasmids The DNA encoding the human MAGI1 gene was subcloned by PCR from the human cDNA clone locus {"type":"entrez-nucleotide","attrs":{"text":"NM_004742","term_id":"66346707"}} NM_004742 (TrueClone Collection, OriGene, Cat No. SC117150).

    Techniques: Protein Concentration, Molecular Weight

    (A) The 1H-15N HSQC spectrum of MAGI1 WW2 355–390, with labels. (*) Signals from the N- and C-terminal artificial tags of the present construct. (B) Solution structures of MAGI1 WW2 355–390, in line representations. (Cyan) Residues in the N- and C-terminal artificial tags of the present construct.

    Journal:

    Article Title: Structural basis for controlling the dimerization and stability of the WW domains of an atypical subfamily

    doi: 10.1110/ps.035329.108

    Figure Lengend Snippet: (A) The 1H-15N HSQC spectrum of MAGI1 WW2 355–390, with labels. (*) Signals from the N- and C-terminal artificial tags of the present construct. (B) Solution structures of MAGI1 WW2 355–390, in line representations. (Cyan) Residues in the N- and C-terminal artificial tags of the present construct.

    Article Snippet: Plasmids The DNA encoding the human MAGI1 gene was subcloned by PCR from the human cDNA clone locus {"type":"entrez-nucleotide","attrs":{"text":"NM_004742","term_id":"66346707"}} NM_004742 (TrueClone Collection, OriGene, Cat No. SC117150).

    Techniques: Construct

    Structural comparison between mSAV1 WW2 231–266 and hMAGI1 WW2 355–390. (A) Structure of SAV1 WW2 231–266. (Lines) Side chains of key aromatic residues (F249, Y252, H256, Y263) buried in the interface of the homodimer; (neon bars) side chains of the polar residues (E242, S246). These side chains are colored to clarify the representation of the molecular interaction. (B) Structure of MAGI1 WW2 355–390. (Lines) Side chains of the aromatic residues (Y373, Y376, H380, Y387); (neon bars) side chains of the polar residues (E366, D370).

    Journal:

    Article Title: Structural basis for controlling the dimerization and stability of the WW domains of an atypical subfamily

    doi: 10.1110/ps.035329.108

    Figure Lengend Snippet: Structural comparison between mSAV1 WW2 231–266 and hMAGI1 WW2 355–390. (A) Structure of SAV1 WW2 231–266. (Lines) Side chains of key aromatic residues (F249, Y252, H256, Y263) buried in the interface of the homodimer; (neon bars) side chains of the polar residues (E242, S246). These side chains are colored to clarify the representation of the molecular interaction. (B) Structure of MAGI1 WW2 355–390. (Lines) Side chains of the aromatic residues (Y373, Y376, H380, Y387); (neon bars) side chains of the polar residues (E366, D370).

    Article Snippet: Plasmids The DNA encoding the human MAGI1 gene was subcloned by PCR from the human cDNA clone locus {"type":"entrez-nucleotide","attrs":{"text":"NM_004742","term_id":"66346707"}} NM_004742 (TrueClone Collection, OriGene, Cat No. SC117150).

    Techniques:

    (A) The 1H-15N HSQC spectrum of MAGI1 WW2 355–401, with labels. (*) Signals from the N- and C-terminal artificial tags of the present construct. (B) Solution structures of MAGI1 WW2 355–401, in line representations. (Cyan) Residues in the N- and C-terminal artificial tags of the present construct.

    Journal:

    Article Title: Structural basis for controlling the dimerization and stability of the WW domains of an atypical subfamily

    doi: 10.1110/ps.035329.108

    Figure Lengend Snippet: (A) The 1H-15N HSQC spectrum of MAGI1 WW2 355–401, with labels. (*) Signals from the N- and C-terminal artificial tags of the present construct. (B) Solution structures of MAGI1 WW2 355–401, in line representations. (Cyan) Residues in the N- and C-terminal artificial tags of the present construct.

    Article Snippet: Plasmids The DNA encoding the human MAGI1 gene was subcloned by PCR from the human cDNA clone locus {"type":"entrez-nucleotide","attrs":{"text":"NM_004742","term_id":"66346707"}} NM_004742 (TrueClone Collection, OriGene, Cat No. SC117150).

    Techniques: Construct

    The 15N spin relaxation profiles of MAGI1 WW2 355–390 (black), MAGI1 WW2 355–401 (red), and MAGI1 WW2 355–390 D370S (green). The heteronuclear NOE (top), longitudinal (R1; middle), and transverse (R2; bottom) relaxation profiles are shown with error bars. (Cyan arrows) β-strands, (red bar) the α-helix of the longer construct, MAGI1 WW2 355–401.

    Journal:

    Article Title: Structural basis for controlling the dimerization and stability of the WW domains of an atypical subfamily

    doi: 10.1110/ps.035329.108

    Figure Lengend Snippet: The 15N spin relaxation profiles of MAGI1 WW2 355–390 (black), MAGI1 WW2 355–401 (red), and MAGI1 WW2 355–390 D370S (green). The heteronuclear NOE (top), longitudinal (R1; middle), and transverse (R2; bottom) relaxation profiles are shown with error bars. (Cyan arrows) β-strands, (red bar) the α-helix of the longer construct, MAGI1 WW2 355–401.

    Article Snippet: Plasmids The DNA encoding the human MAGI1 gene was subcloned by PCR from the human cDNA clone locus {"type":"entrez-nucleotide","attrs":{"text":"NM_004742","term_id":"66346707"}} NM_004742 (TrueClone Collection, OriGene, Cat No. SC117150).

    Techniques: Construct

    Thermal stability summary of MAGI1 WW2 355–390 and its variants

    Journal:

    Article Title: Structural basis for controlling the dimerization and stability of the WW domains of an atypical subfamily

    doi: 10.1110/ps.035329.108

    Figure Lengend Snippet: Thermal stability summary of MAGI1 WW2 355–390 and its variants

    Article Snippet: Plasmids The DNA encoding the human MAGI1 gene was subcloned by PCR from the human cDNA clone locus {"type":"entrez-nucleotide","attrs":{"text":"NM_004742","term_id":"66346707"}} NM_004742 (TrueClone Collection, OriGene, Cat No. SC117150).

    Techniques:

    (A) Far-UV CD spectra of MAGI1 WW2 355–390 (black), MAGI1 WW2 355–401 (red), and MAGI1 WW2 355–390 D370S (green), recorded at 20°C. (B) Thermal denaturation profiles of MAGI1 WW2 355–390 (black), MAGI1 WW2 355–401 (red), and those of the D370S mutant, recorded with 55 μM (green) and 5 μM (blue) protein concentrations. The changes in ellipticity at 232 nm for MAGI1 WW2 355–390 and MAGI1 WW2 355–390 D370S, and that at 217 nm for MAGI1 WW2 355–401, were monitored and analyzed as a function of temperature.

    Journal:

    Article Title: Structural basis for controlling the dimerization and stability of the WW domains of an atypical subfamily

    doi: 10.1110/ps.035329.108

    Figure Lengend Snippet: (A) Far-UV CD spectra of MAGI1 WW2 355–390 (black), MAGI1 WW2 355–401 (red), and MAGI1 WW2 355–390 D370S (green), recorded at 20°C. (B) Thermal denaturation profiles of MAGI1 WW2 355–390 (black), MAGI1 WW2 355–401 (red), and those of the D370S mutant, recorded with 55 μM (green) and 5 μM (blue) protein concentrations. The changes in ellipticity at 232 nm for MAGI1 WW2 355–390 and MAGI1 WW2 355–390 D370S, and that at 217 nm for MAGI1 WW2 355–401, were monitored and analyzed as a function of temperature.

    Article Snippet: Plasmids The DNA encoding the human MAGI1 gene was subcloned by PCR from the human cDNA clone locus {"type":"entrez-nucleotide","attrs":{"text":"NM_004742","term_id":"66346707"}} NM_004742 (TrueClone Collection, OriGene, Cat No. SC117150).

    Techniques: Mutagenesis

    (A) Close-up view highlighting the interactions around the C-terminal α-helix in MAGI1 WW2 355–401. Key residues described in the main text are marked. (B) Structural comparison between MAGI1 WW2 355–390 (blue) and MAGI1 WW2 355–401 (red). Structures were superimposed using the backbone heavy atoms in the region between Leu361 and Pro390. (C) Comparison of the accessible surface areas of the residues between MAGI1 WW2 355–390 (black) and MAGI1 WW2 355–401 (red). (Cyan bars) β-strands; (red bar) the α-helix of the longer construct, MAGI1 WW2 355–401.

    Journal:

    Article Title: Structural basis for controlling the dimerization and stability of the WW domains of an atypical subfamily

    doi: 10.1110/ps.035329.108

    Figure Lengend Snippet: (A) Close-up view highlighting the interactions around the C-terminal α-helix in MAGI1 WW2 355–401. Key residues described in the main text are marked. (B) Structural comparison between MAGI1 WW2 355–390 (blue) and MAGI1 WW2 355–401 (red). Structures were superimposed using the backbone heavy atoms in the region between Leu361 and Pro390. (C) Comparison of the accessible surface areas of the residues between MAGI1 WW2 355–390 (black) and MAGI1 WW2 355–401 (red). (Cyan bars) β-strands; (red bar) the α-helix of the longer construct, MAGI1 WW2 355–401.

    Article Snippet: Plasmids The DNA encoding the human MAGI1 gene was subcloned by PCR from the human cDNA clone locus {"type":"entrez-nucleotide","attrs":{"text":"NM_004742","term_id":"66346707"}} NM_004742 (TrueClone Collection, OriGene, Cat No. SC117150).

    Techniques: Construct

    (A) The neighbor-joining (NJ) tree dendrogram of the WW domains from human origin. The WW domain sequences from human origin were obtained from the Pfam server (http://www.sanger.ac.uk/Software/Pfam/), and the redundancy was removed using the 100% sequence identity filter. The sequences thus selected were analyzed using the program CLUSTAL W (Thompson et al. 1994). (Magenta) The members of the subclass that contains SAV1 WW2 and MAGI1 WW2. (B) Comparative representation of the LOGO plot of the representative WW domain sequences and the sequences of the members of the subclass that contains SAV1 WW2 and MAG1 WW2. (Yellow boxes) Polar residues of E242 and S246 in SAV1 WW2, as well as those of their counterparts in MAGI1 WW2, E366 and D370. (Red) Acidic residues, (blue) basic residues.

    Journal:

    Article Title: Structural basis for controlling the dimerization and stability of the WW domains of an atypical subfamily

    doi: 10.1110/ps.035329.108

    Figure Lengend Snippet: (A) The neighbor-joining (NJ) tree dendrogram of the WW domains from human origin. The WW domain sequences from human origin were obtained from the Pfam server (http://www.sanger.ac.uk/Software/Pfam/), and the redundancy was removed using the 100% sequence identity filter. The sequences thus selected were analyzed using the program CLUSTAL W (Thompson et al. 1994). (Magenta) The members of the subclass that contains SAV1 WW2 and MAGI1 WW2. (B) Comparative representation of the LOGO plot of the representative WW domain sequences and the sequences of the members of the subclass that contains SAV1 WW2 and MAG1 WW2. (Yellow boxes) Polar residues of E242 and S246 in SAV1 WW2, as well as those of their counterparts in MAGI1 WW2, E366 and D370. (Red) Acidic residues, (blue) basic residues.

    Article Snippet: Plasmids The DNA encoding the human MAGI1 gene was subcloned by PCR from the human cDNA clone locus NM_004742 (TrueClone Collection, OriGene, Cat No. SC117150).

    Techniques: Software, Sequencing

    Equilibrium analytical ultracentrifugation of MAGI1 WW2 355–390. (Bottom panel) Radial distribution of the absorbance in the centrifuge cell at equilibrium at 16,000 rpm, with a protein concentration of 0.5 mg/mL. The solid line through the data represents the fit to a single species with a molecular weight corresponding to 5611, while the theoretical molecular weight for the single polypeptide chain is 5580. (Upper panels) Residuals for the fit.

    Journal:

    Article Title: Structural basis for controlling the dimerization and stability of the WW domains of an atypical subfamily

    doi: 10.1110/ps.035329.108

    Figure Lengend Snippet: Equilibrium analytical ultracentrifugation of MAGI1 WW2 355–390. (Bottom panel) Radial distribution of the absorbance in the centrifuge cell at equilibrium at 16,000 rpm, with a protein concentration of 0.5 mg/mL. The solid line through the data represents the fit to a single species with a molecular weight corresponding to 5611, while the theoretical molecular weight for the single polypeptide chain is 5580. (Upper panels) Residuals for the fit.

    Article Snippet: Plasmids The DNA encoding the human MAGI1 gene was subcloned by PCR from the human cDNA clone locus NM_004742 (TrueClone Collection, OriGene, Cat No. SC117150).

    Techniques: Analytical Ultracentrifugation, Protein Concentration, Molecular Weight

    (A) The 1H-15N HSQC spectrum of MAGI1 WW2 355–390, with labels. (*) Signals from the N- and C-terminal artificial tags of the present construct. (B) Solution structures of MAGI1 WW2 355–390, in line representations. (Cyan) Residues in the N- and C-terminal artificial tags of the present construct.

    Journal:

    Article Title: Structural basis for controlling the dimerization and stability of the WW domains of an atypical subfamily

    doi: 10.1110/ps.035329.108

    Figure Lengend Snippet: (A) The 1H-15N HSQC spectrum of MAGI1 WW2 355–390, with labels. (*) Signals from the N- and C-terminal artificial tags of the present construct. (B) Solution structures of MAGI1 WW2 355–390, in line representations. (Cyan) Residues in the N- and C-terminal artificial tags of the present construct.

    Article Snippet: Plasmids The DNA encoding the human MAGI1 gene was subcloned by PCR from the human cDNA clone locus NM_004742 (TrueClone Collection, OriGene, Cat No. SC117150).

    Techniques: Construct

    Structural comparison between mSAV1 WW2 231–266 and hMAGI1 WW2 355–390. (A) Structure of SAV1 WW2 231–266. (Lines) Side chains of key aromatic residues (F249, Y252, H256, Y263) buried in the interface of the homodimer; (neon bars) side chains of the polar residues (E242, S246). These side chains are colored to clarify the representation of the molecular interaction. (B) Structure of MAGI1 WW2 355–390. (Lines) Side chains of the aromatic residues (Y373, Y376, H380, Y387); (neon bars) side chains of the polar residues (E366, D370).

    Journal:

    Article Title: Structural basis for controlling the dimerization and stability of the WW domains of an atypical subfamily

    doi: 10.1110/ps.035329.108

    Figure Lengend Snippet: Structural comparison between mSAV1 WW2 231–266 and hMAGI1 WW2 355–390. (A) Structure of SAV1 WW2 231–266. (Lines) Side chains of key aromatic residues (F249, Y252, H256, Y263) buried in the interface of the homodimer; (neon bars) side chains of the polar residues (E242, S246). These side chains are colored to clarify the representation of the molecular interaction. (B) Structure of MAGI1 WW2 355–390. (Lines) Side chains of the aromatic residues (Y373, Y376, H380, Y387); (neon bars) side chains of the polar residues (E366, D370).

    Article Snippet: Plasmids The DNA encoding the human MAGI1 gene was subcloned by PCR from the human cDNA clone locus NM_004742 (TrueClone Collection, OriGene, Cat No. SC117150).

    Techniques: Comparison

    (A) The 1H-15N HSQC spectrum of MAGI1 WW2 355–401, with labels. (*) Signals from the N- and C-terminal artificial tags of the present construct. (B) Solution structures of MAGI1 WW2 355–401, in line representations. (Cyan) Residues in the N- and C-terminal artificial tags of the present construct.

    Journal:

    Article Title: Structural basis for controlling the dimerization and stability of the WW domains of an atypical subfamily

    doi: 10.1110/ps.035329.108

    Figure Lengend Snippet: (A) The 1H-15N HSQC spectrum of MAGI1 WW2 355–401, with labels. (*) Signals from the N- and C-terminal artificial tags of the present construct. (B) Solution structures of MAGI1 WW2 355–401, in line representations. (Cyan) Residues in the N- and C-terminal artificial tags of the present construct.

    Article Snippet: Plasmids The DNA encoding the human MAGI1 gene was subcloned by PCR from the human cDNA clone locus NM_004742 (TrueClone Collection, OriGene, Cat No. SC117150).

    Techniques: Construct

    The 15N spin relaxation profiles of MAGI1 WW2 355–390 (black), MAGI1 WW2 355–401 (red), and MAGI1 WW2 355–390 D370S (green). The heteronuclear NOE (top), longitudinal (R1; middle), and transverse (R2; bottom) relaxation profiles are shown with error bars. (Cyan arrows) β-strands, (red bar) the α-helix of the longer construct, MAGI1 WW2 355–401.

    Journal:

    Article Title: Structural basis for controlling the dimerization and stability of the WW domains of an atypical subfamily

    doi: 10.1110/ps.035329.108

    Figure Lengend Snippet: The 15N spin relaxation profiles of MAGI1 WW2 355–390 (black), MAGI1 WW2 355–401 (red), and MAGI1 WW2 355–390 D370S (green). The heteronuclear NOE (top), longitudinal (R1; middle), and transverse (R2; bottom) relaxation profiles are shown with error bars. (Cyan arrows) β-strands, (red bar) the α-helix of the longer construct, MAGI1 WW2 355–401.

    Article Snippet: Plasmids The DNA encoding the human MAGI1 gene was subcloned by PCR from the human cDNA clone locus NM_004742 (TrueClone Collection, OriGene, Cat No. SC117150).

    Techniques: Construct

    Thermal stability summary of MAGI1 WW2 355–390 and its variants

    Journal:

    Article Title: Structural basis for controlling the dimerization and stability of the WW domains of an atypical subfamily

    doi: 10.1110/ps.035329.108

    Figure Lengend Snippet: Thermal stability summary of MAGI1 WW2 355–390 and its variants

    Article Snippet: Plasmids The DNA encoding the human MAGI1 gene was subcloned by PCR from the human cDNA clone locus NM_004742 (TrueClone Collection, OriGene, Cat No. SC117150).

    Techniques:

    (A) Far-UV CD spectra of MAGI1 WW2 355–390 (black), MAGI1 WW2 355–401 (red), and MAGI1 WW2 355–390 D370S (green), recorded at 20°C. (B) Thermal denaturation profiles of MAGI1 WW2 355–390 (black), MAGI1 WW2 355–401 (red), and those of the D370S mutant, recorded with 55 μM (green) and 5 μM (blue) protein concentrations. The changes in ellipticity at 232 nm for MAGI1 WW2 355–390 and MAGI1 WW2 355–390 D370S, and that at 217 nm for MAGI1 WW2 355–401, were monitored and analyzed as a function of temperature.

    Journal:

    Article Title: Structural basis for controlling the dimerization and stability of the WW domains of an atypical subfamily

    doi: 10.1110/ps.035329.108

    Figure Lengend Snippet: (A) Far-UV CD spectra of MAGI1 WW2 355–390 (black), MAGI1 WW2 355–401 (red), and MAGI1 WW2 355–390 D370S (green), recorded at 20°C. (B) Thermal denaturation profiles of MAGI1 WW2 355–390 (black), MAGI1 WW2 355–401 (red), and those of the D370S mutant, recorded with 55 μM (green) and 5 μM (blue) protein concentrations. The changes in ellipticity at 232 nm for MAGI1 WW2 355–390 and MAGI1 WW2 355–390 D370S, and that at 217 nm for MAGI1 WW2 355–401, were monitored and analyzed as a function of temperature.

    Article Snippet: Plasmids The DNA encoding the human MAGI1 gene was subcloned by PCR from the human cDNA clone locus NM_004742 (TrueClone Collection, OriGene, Cat No. SC117150).

    Techniques: Circular Dichroism, Mutagenesis

    (A) Close-up view highlighting the interactions around the C-terminal α-helix in MAGI1 WW2 355–401. Key residues described in the main text are marked. (B) Structural comparison between MAGI1 WW2 355–390 (blue) and MAGI1 WW2 355–401 (red). Structures were superimposed using the backbone heavy atoms in the region between Leu361 and Pro390. (C) Comparison of the accessible surface areas of the residues between MAGI1 WW2 355–390 (black) and MAGI1 WW2 355–401 (red). (Cyan bars) β-strands; (red bar) the α-helix of the longer construct, MAGI1 WW2 355–401.

    Journal:

    Article Title: Structural basis for controlling the dimerization and stability of the WW domains of an atypical subfamily

    doi: 10.1110/ps.035329.108

    Figure Lengend Snippet: (A) Close-up view highlighting the interactions around the C-terminal α-helix in MAGI1 WW2 355–401. Key residues described in the main text are marked. (B) Structural comparison between MAGI1 WW2 355–390 (blue) and MAGI1 WW2 355–401 (red). Structures were superimposed using the backbone heavy atoms in the region between Leu361 and Pro390. (C) Comparison of the accessible surface areas of the residues between MAGI1 WW2 355–390 (black) and MAGI1 WW2 355–401 (red). (Cyan bars) β-strands; (red bar) the α-helix of the longer construct, MAGI1 WW2 355–401.

    Article Snippet: Plasmids The DNA encoding the human MAGI1 gene was subcloned by PCR from the human cDNA clone locus NM_004742 (TrueClone Collection, OriGene, Cat No. SC117150).

    Techniques: Comparison, Construct