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Biomatik sh2 domains

Phosphorylation of Tyr 1510 of IQGAP1 creates a docking site for <t>SH2</t> domains. ( A ). A peptide array containing 124 different GST-tagged recombinant SH2 protein domains, each spotted in duplicate, was generated as detailed in Materials and Methods . GST alone was spotted on the array as the negative control. Biotinylated peptides comprising residues 1502–1518 of IQGAP1 with phosphorylated Tyr 1510 (pTyr 1510 ) were labeled with fluorescent streptavidin and incubated with the array for 16 h at 4 °C. After washing, fluorescence from the bound peptides (green dots) was detected. The red and orange circles delineate the duplicates for the SH2 domains of Abl1 and Abl2, respectively. ( B ). Similar analysis was conducted with the same IQGAP1 peptide, except Tyr 1510 was not phosphorylated. ( C ). The peptide array was probed with anti-GST antibody to show the positions and loading of the GST-SH2 domains and control GST.

Sh2 Domains, supplied by Biomatik, 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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1) Product Images from "IQGAP1 Is a Phosphotyrosine-Regulated Scaffold for SH2-Containing Proteins"

Article Title: IQGAP1 Is a Phosphotyrosine-Regulated Scaffold for SH2-Containing Proteins

Journal: Cells

doi: 10.3390/cells12030483

Phosphorylation of Tyr 1510 of IQGAP1 creates a docking site for SH2 domains. ( A ). A peptide array containing 124 different GST-tagged recombinant SH2 protein domains, each spotted in duplicate, was generated as detailed in Materials and Methods . GST alone was spotted on the array as the negative control. Biotinylated peptides comprising residues 1502–1518 of IQGAP1 with phosphorylated Tyr 1510 (pTyr 1510 ) were labeled with fluorescent streptavidin and incubated with the array for 16 h at 4 °C. After washing, fluorescence from the bound peptides (green dots) was detected. The red and orange circles delineate the duplicates for the SH2 domains of Abl1 and Abl2, respectively. ( B ). Similar analysis was conducted with the same IQGAP1 peptide, except Tyr 1510 was not phosphorylated. ( C ). The peptide array was probed with anti-GST antibody to show the positions and loading of the GST-SH2 domains and control GST.

Figure Legend Snippet: Phosphorylation of Tyr 1510 of IQGAP1 creates a docking site for SH2 domains. ( A ). A peptide array containing 124 different GST-tagged recombinant SH2 protein domains, each spotted in duplicate, was generated as detailed in Materials and Methods . GST alone was spotted on the array as the negative control. Biotinylated peptides comprising residues 1502–1518 of IQGAP1 with phosphorylated Tyr 1510 (pTyr 1510 ) were labeled with fluorescent streptavidin and incubated with the array for 16 h at 4 °C. After washing, fluorescence from the bound peptides (green dots) was detected. The red and orange circles delineate the duplicates for the SH2 domains of Abl1 and Abl2, respectively. ( B ). Similar analysis was conducted with the same IQGAP1 peptide, except Tyr 1510 was not phosphorylated. ( C ). The peptide array was probed with anti-GST antibody to show the positions and loading of the GST-SH2 domains and control GST.

Techniques Used: Phospho-proteomics, Peptide Microarray, Recombinant, Generated, Negative Control, Labeling, Incubation, Fluorescence, Control

$The SH2 domains of Abl1 and Abl2 bind directly to tyrosine-phosphorylated IQGAP1. ( A ). Quantification of the fluorescence intensity of the IQGAP1 peptides with unphosphorylated (Tyr 1510 , pale green bars) or phosphorylated (pTyr 1510 , dark green bars) Tyr 1510 bound to the SH2 domains of Abl1 or Abl2 on the SH2 array. Binding to GST is the control. Data represent the mean fluorescence from two duplicates. a.u., arbitrary units. ( B ). H1993 cells were incubated with 100 nM crizotinib (criz, + ) or vehicle DMSO (−). After 24 h, cells were lysed and equal amounts of protein lysate were incubated with the purified GST-SH2 domains of Abl1 or Abl2 bound to glutathione-Sepharose. Control pull-downs were carried out with GST-glutathione-Sepharose. After washing, proteins attached to the beads were eluted in Laemmli sample buffer and analyzed by Western blotting. The membrane was probed with anti-IQGAP1 (IQ1) and anti-GST antibodies. Input designates unfractionated cell lysates. Both panels are from the same membrane. Blots are representative of two independent experiments. The full blots of the two replicates are shown in . ( C ). The IQGAP1 bands observed after pull-down were quantified using Image Studio 2.0 (LI-COR Biosciences). The intensity of IQGAP1 in DMSO-treated cells was set as 1. Data are presented as the means of two independent replicates. ( D ). Purified GST-IQGAP1 (IQ1) on glutathione-Sepharose was incubated with purified active MET in the presence (+ATP) or absence (−ATP) of ATP. After washing, beads were incubated with 2 μg of purified Abl1 (left panel) or Abl2 (right panel). Control pull-downs were carried out with GST-Sepharose. After washing, proteins attached to the beads were eluted in Laemmli sample buffer and analyzed by SDS-PAGE and Western blotting. The membrane was probed with anti-IQGAP1 (IQ1), anti-phosphotyrosine (pTyr), and anti-Abl1 or anti-Abl2 antibodies. The overlap between IQGAP1 (red) and pTyr (green) signals is visible in the merged image (yellow). Input designates pure Abl1 or Abl2 not subjected to pull-down. The blots are representative of three independent experiments. The full blots of the three replicates are shown in . ( E ). The Abl1 and Abl2 bands observed after pull-down by GST-IQGAP1 were quantified using Image Studio 2.0 (LI-COR Biosciences). The intensity of Abl1 and Abl2 signals observed with non-phosphorylated IQGAP1 (−ATP) was set as 1. Data are the means ± SD of three independent experiments. Statistical analyses were performed with unpaired t -tests (*, p ≤ 0.05).$
Figure Legend Snippet: The SH2 domains of Abl1 and Abl2 bind directly to tyrosine-phosphorylated IQGAP1. ( A ). Quantification of the fluorescence intensity of the IQGAP1 peptides with unphosphorylated (Tyr 1510 , pale green bars) or phosphorylated (pTyr 1510 , dark green bars) Tyr 1510 bound to the SH2 domains of Abl1 or Abl2 on the SH2 array. Binding to GST is the control. Data represent the mean fluorescence from two duplicates. a.u., arbitrary units. ( B ). H1993 cells were incubated with 100 nM crizotinib (criz, + ) or vehicle DMSO (−). After 24 h, cells were lysed and equal amounts of protein lysate were incubated with the purified GST-SH2 domains of Abl1 or Abl2 bound to glutathione-Sepharose. Control pull-downs were carried out with GST-glutathione-Sepharose. After washing, proteins attached to the beads were eluted in Laemmli sample buffer and analyzed by Western blotting. The membrane was probed with anti-IQGAP1 (IQ1) and anti-GST antibodies. Input designates unfractionated cell lysates. Both panels are from the same membrane. Blots are representative of two independent experiments. The full blots of the two replicates are shown in . ( C ). The IQGAP1 bands observed after pull-down were quantified using Image Studio 2.0 (LI-COR Biosciences). The intensity of IQGAP1 in DMSO-treated cells was set as 1. Data are presented as the means of two independent replicates. ( D ). Purified GST-IQGAP1 (IQ1) on glutathione-Sepharose was incubated with purified active MET in the presence (+ATP) or absence (−ATP) of ATP. After washing, beads were incubated with 2 μg of purified Abl1 (left panel) or Abl2 (right panel). Control pull-downs were carried out with GST-Sepharose. After washing, proteins attached to the beads were eluted in Laemmli sample buffer and analyzed by SDS-PAGE and Western blotting. The membrane was probed with anti-IQGAP1 (IQ1), anti-phosphotyrosine (pTyr), and anti-Abl1 or anti-Abl2 antibodies. The overlap between IQGAP1 (red) and pTyr (green) signals is visible in the merged image (yellow). Input designates pure Abl1 or Abl2 not subjected to pull-down. The blots are representative of three independent experiments. The full blots of the three replicates are shown in . ( E ). The Abl1 and Abl2 bands observed after pull-down by GST-IQGAP1 were quantified using Image Studio 2.0 (LI-COR Biosciences). The intensity of Abl1 and Abl2 signals observed with non-phosphorylated IQGAP1 (−ATP) was set as 1. Data are the means ± SD of three independent experiments. Statistical analyses were performed with unpaired t -tests (*, p ≤ 0.05).

Techniques Used: Fluorescence, Binding Assay, Control, Incubation, Purification, Western Blot, Membrane, SDS Page

Model of IQGAP1 in receptor tyrosine kinase signaling. ( A ). Schematic of IQGAP1 that highlights known post-translational modifications. The five domains are CHD (calponin-homology domain), WW, IQ, GRD (GAP-related domain), and RGCT (RasGAP_C-terminus). Post-translational modifications that have been characterized on IQGAP1 are shown below the modified amino acid. The identified domain to which receptor tyrosine kinases bind is depicted above IQGAP1. Phosphorylation of IQGAP1 on Tyr 1510 , leading to the recruitment of SH2 domains, is also shown. ( B ). Model depicting the identified modes of action of IQGAP1 in receptor tyrosine kinase signaling. Upper panel: constitutive scaffolding by IQGAP1. IQGAP1 binds constitutively to both the growth factor receptor and a downstream signaling protein. (i) Ligand binding activates the receptor. (ii) Scaffolding by IQGAP1 facilitates activation of the signaling protein by the activated receptor, initiating downstream signaling. (iii) Signal transduction from the activated receptor to the effector protein does not occur in the absence of scaffolding by IQGAP1. The mode of action depicted here is for the EGF receptor (EGFR) and B-Raf kinase in activation of the MAPK cascade [ , ]. Lower panel: phosphotyrosine-dependent scaffolding by IQGAP1. (i) Phosphorylation of tyrosine on IQGAP1 by an activated receptor tyrosine kinase (ii) initiates recruitment of selected SH2-containing proteins. The mechanism illustrated here is for the MET receptor tyrosine kinase and the SH2-containing proteins Abl1 and Abl2. In this example, IQGAP1 (iii) impairs MET activation and signaling and (iv) decreases HGF-stimulated signaling of Abl to the adaptor protein CrkL. Therefore, IQGAP1 functions as a rheostat regulating the flux of signaling between activated MET receptors and SH2-containing signaling proteins. (v) Recruitment of SH2-containing proteins does not occur in the absence of receptor tyrosine kinase-catalyzed phosphorylation of IQGAP1. Abbreviations: EGF, epidermal growth factor; EGFR, EGF receptor; HER2, human epidermal growth factor receptor 2; HGF, hepatocyte growth factor; IR, insulin receptor; P, phosphate; pS, serine phosphorylation; pY, tyrosine phosphorylation; SUMO, SUMOylation; Ub, ubiquitination.

Figure Legend Snippet: Model of IQGAP1 in receptor tyrosine kinase signaling. ( A ). Schematic of IQGAP1 that highlights known post-translational modifications. The five domains are CHD (calponin-homology domain), WW, IQ, GRD (GAP-related domain), and RGCT (RasGAP_C-terminus). Post-translational modifications that have been characterized on IQGAP1 are shown below the modified amino acid. The identified domain to which receptor tyrosine kinases bind is depicted above IQGAP1. Phosphorylation of IQGAP1 on Tyr 1510 , leading to the recruitment of SH2 domains, is also shown. ( B ). Model depicting the identified modes of action of IQGAP1 in receptor tyrosine kinase signaling. Upper panel: constitutive scaffolding by IQGAP1. IQGAP1 binds constitutively to both the growth factor receptor and a downstream signaling protein. (i) Ligand binding activates the receptor. (ii) Scaffolding by IQGAP1 facilitates activation of the signaling protein by the activated receptor, initiating downstream signaling. (iii) Signal transduction from the activated receptor to the effector protein does not occur in the absence of scaffolding by IQGAP1. The mode of action depicted here is for the EGF receptor (EGFR) and B-Raf kinase in activation of the MAPK cascade [ , ]. Lower panel: phosphotyrosine-dependent scaffolding by IQGAP1. (i) Phosphorylation of tyrosine on IQGAP1 by an activated receptor tyrosine kinase (ii) initiates recruitment of selected SH2-containing proteins. The mechanism illustrated here is for the MET receptor tyrosine kinase and the SH2-containing proteins Abl1 and Abl2. In this example, IQGAP1 (iii) impairs MET activation and signaling and (iv) decreases HGF-stimulated signaling of Abl to the adaptor protein CrkL. Therefore, IQGAP1 functions as a rheostat regulating the flux of signaling between activated MET receptors and SH2-containing signaling proteins. (v) Recruitment of SH2-containing proteins does not occur in the absence of receptor tyrosine kinase-catalyzed phosphorylation of IQGAP1. Abbreviations: EGF, epidermal growth factor; EGFR, EGF receptor; HER2, human epidermal growth factor receptor 2; HGF, hepatocyte growth factor; IR, insulin receptor; P, phosphate; pS, serine phosphorylation; pY, tyrosine phosphorylation; SUMO, SUMOylation; Ub, ubiquitination.

Techniques Used: Modification, Phospho-proteomics, Scaffolding, Ligand Binding Assay, Activation Assay, Transduction, Ubiquitin Proteomics

Image Search Results

Src SH2 binding to cortactin does not involve tyrosine phosphorylation and binds cortactin repeats 1 and 5. (A) GST and GST-Src SH2 affinity precipitation from MTLn3 cells evaluated for cortactin tyrosine phosphorylation. The ratio of phosphorylated cortactin levels and the normalized amounts of total precipitated cortactin are indicated. (B) Src SH2 far western analysis of FLAG-tagged recombinant wild-type and cortactin phosphorylation mutants. TYM, triple tyrosine mutant. (C) Affinity precipitation analysis of FLAG-tagged recombinant wild-type and cortactin phosphorylation mutants from extracts with GST-Src SH2 domain. (D) Affinity precipitation of non-phosphorylated, recombinant cortactin with GST and GST-Src SH2. Normalized intensity levels are shown relative to GST control. (E) GST-SH2 domain far western blotting of the cortactin NTA and repeats region. CT, C terminus; LC, IgG light chain; NT, N terminus. Arrows denote position of IgG heavy chain (HC) recognized by cross reactivity with secondary antibodies during the blotting process. Asterisks indicate the positions of recombinant cortactin proteins. (F) GST-SH2 far western analysis of cortactin deletion cortactin constructs. (G) Far western binding of the GST-Src SH2 domain to tandem cortactin repeat chimeric constructs.

Journal: Journal of Cell Science

Article Title: Src binds cortactin through an SH2 domain cystine-mediated linkage

doi: 10.1242/jcs.121046

Figure Lengend Snippet: Src SH2 binding to cortactin does not involve tyrosine phosphorylation and binds cortactin repeats 1 and 5. (A) GST and GST-Src SH2 affinity precipitation from MTLn3 cells evaluated for cortactin tyrosine phosphorylation. The ratio of phosphorylated cortactin levels and the normalized amounts of total precipitated cortactin are indicated. (B) Src SH2 far western analysis of FLAG-tagged recombinant wild-type and cortactin phosphorylation mutants. TYM, triple tyrosine mutant. (C) Affinity precipitation analysis of FLAG-tagged recombinant wild-type and cortactin phosphorylation mutants from extracts with GST-Src SH2 domain. (D) Affinity precipitation of non-phosphorylated, recombinant cortactin with GST and GST-Src SH2. Normalized intensity levels are shown relative to GST control. (E) GST-SH2 domain far western blotting of the cortactin NTA and repeats region. CT, C terminus; LC, IgG light chain; NT, N terminus. Arrows denote position of IgG heavy chain (HC) recognized by cross reactivity with secondary antibodies during the blotting process. Asterisks indicate the positions of recombinant cortactin proteins. (F) GST-SH2 far western analysis of cortactin deletion cortactin constructs. (G) Far western binding of the GST-Src SH2 domain to tandem cortactin repeat chimeric constructs.

Article Snippet: Screening of TransignalTM SH2 Domain Arrays (Panomics Cat. NO. MA3040) was conducted using 1.0 mg of each cortactin peptide according to the manufacturer's protocol.

Techniques: Binding Assay, Phospho-proteomics, Affinity Precipitation, Western Blot, Recombinant, Mutagenesis, Control, Far Western Blot, Construct

Cortactin cysteines 112 and 246 are required for Src SH2 domain binding. (A) Alignment of cortactin repeats denoting C112 and C246. (B,C) Far western blotting of GST-Src SH2 domain with cortactin cysteine to alanine mutants. CT, C terminus; HC, IgG heavy chain; LC, IgG light chain; NT, N terminus; WT; full-length wild-type cortactin. Dashed line separates HC from chimeric cortactin proteins (asterisks) due to similar molecular weights. (D) Far western analysis of Src SH2 domain binding to the C112/C246A cortactin double cysteine mutant (DCM). (E) Affinity precipitation analysis of Src SH2 domain binding to the C112/C246A cortactin double cysteine mutant (DCM).

Journal: Journal of Cell Science

Article Title: Src binds cortactin through an SH2 domain cystine-mediated linkage

doi: 10.1242/jcs.121046

Figure Lengend Snippet: Cortactin cysteines 112 and 246 are required for Src SH2 domain binding. (A) Alignment of cortactin repeats denoting C112 and C246. (B,C) Far western blotting of GST-Src SH2 domain with cortactin cysteine to alanine mutants. CT, C terminus; HC, IgG heavy chain; LC, IgG light chain; NT, N terminus; WT; full-length wild-type cortactin. Dashed line separates HC from chimeric cortactin proteins (asterisks) due to similar molecular weights. (D) Far western analysis of Src SH2 domain binding to the C112/C246A cortactin double cysteine mutant (DCM). (E) Affinity precipitation analysis of Src SH2 domain binding to the C112/C246A cortactin double cysteine mutant (DCM).

Article Snippet: Screening of TransignalTM SH2 Domain Arrays (Panomics Cat. NO. MA3040) was conducted using 1.0 mg of each cortactin peptide according to the manufacturer's protocol.

Techniques: Binding Assay, Far Western Blot, Western Blot, Mutagenesis, Affinity Precipitation

Cysteine-containing cortactin peptides dock within the Src SH2 phosphotyrosine binding region. (A) Molecular modelling of the Src SH2 domain with phosphorylated Src and cortactin pentapeptides. Enlarged views show position of Src R175, Src C185 and the respective central Src or cortactin peptide residues. (B) Calculated binding energies for each peptide docking condition shown in (A).

Journal: Journal of Cell Science

Article Title: Src binds cortactin through an SH2 domain cystine-mediated linkage

doi: 10.1242/jcs.121046

Figure Lengend Snippet: Cysteine-containing cortactin peptides dock within the Src SH2 phosphotyrosine binding region. (A) Molecular modelling of the Src SH2 domain with phosphorylated Src and cortactin pentapeptides. Enlarged views show position of Src R175, Src C185 and the respective central Src or cortactin peptide residues. (B) Calculated binding energies for each peptide docking condition shown in (A).

Article Snippet: Screening of TransignalTM SH2 Domain Arrays (Panomics Cat. NO. MA3040) was conducted using 1.0 mg of each cortactin peptide according to the manufacturer's protocol.

Techniques: Binding Assay

Binding and phosphorylation of cortactin by Src is redox dependent and requires Src C185. (A) Co-immunoprecipitation (IP) of cortactin with Src followed by analysis under reducing (R) and non-reducing (NR) conditions. Asterisks denote equivalent bands in cortactin and Src immunoblots. (B) Co-immunoprecipitation of Src with cortactin followed by analysis under reducing (R) and non-reducing (NR) conditions. Asterisks denote equivalent bands in cortactin and Src immunoblots. (C) Phosphorylation of cortactin by Src in the absence and presence of DTT. (D) Far western analysis of GST-Src SH2 and C185A. (E) Affinity precipitation analysis of FAK and cortactin binding to GST-Src SH2 C185A.

Journal: Journal of Cell Science

Article Title: Src binds cortactin through an SH2 domain cystine-mediated linkage

doi: 10.1242/jcs.121046

Figure Lengend Snippet: Binding and phosphorylation of cortactin by Src is redox dependent and requires Src C185. (A) Co-immunoprecipitation (IP) of cortactin with Src followed by analysis under reducing (R) and non-reducing (NR) conditions. Asterisks denote equivalent bands in cortactin and Src immunoblots. (B) Co-immunoprecipitation of Src with cortactin followed by analysis under reducing (R) and non-reducing (NR) conditions. Asterisks denote equivalent bands in cortactin and Src immunoblots. (C) Phosphorylation of cortactin by Src in the absence and presence of DTT. (D) Far western analysis of GST-Src SH2 and C185A. (E) Affinity precipitation analysis of FAK and cortactin binding to GST-Src SH2 C185A.

Article Snippet: Screening of TransignalTM SH2 Domain Arrays (Panomics Cat. NO. MA3040) was conducted using 1.0 mg of each cortactin peptide according to the manufacturer's protocol.

Techniques: Binding Assay, Phospho-proteomics, Immunoprecipitation, Western Blot, Affinity Precipitation

Src C185 forms a cystine bond with cortactin C112 and C246. (A) Sequence of the predicted Src SH2 domain tryptic fragment containing C185. Predicted cystine bonding between Src C185 and the cortactin C112 and C246 tryptic peptides with predicted masses are shown below. (B–D) Extracted ion chromatogram (left) and ion fragmentation spectra (right) from tandem LC-MS/MS of the GST-Src SH2 domain (B), the GST-SH2 domain with the cortactin C112 peptide (C) and the GST-SH2 domain with cortactin C246 peptide (D). Spectra were enlarged to indicate the position of the Src C185 b4 ion (boxed in red).

Journal: Journal of Cell Science

Article Title: Src binds cortactin through an SH2 domain cystine-mediated linkage

doi: 10.1242/jcs.121046

Figure Lengend Snippet: Src C185 forms a cystine bond with cortactin C112 and C246. (A) Sequence of the predicted Src SH2 domain tryptic fragment containing C185. Predicted cystine bonding between Src C185 and the cortactin C112 and C246 tryptic peptides with predicted masses are shown below. (B–D) Extracted ion chromatogram (left) and ion fragmentation spectra (right) from tandem LC-MS/MS of the GST-Src SH2 domain (B), the GST-SH2 domain with the cortactin C112 peptide (C) and the GST-SH2 domain with cortactin C246 peptide (D). Spectra were enlarged to indicate the position of the Src C185 b4 ion (boxed in red).

Article Snippet: Screening of TransignalTM SH2 Domain Arrays (Panomics Cat. NO. MA3040) was conducted using 1.0 mg of each cortactin peptide according to the manufacturer's protocol.

Techniques: Sequencing, Liquid Chromatography with Mass Spectroscopy

Observed and predicted ion masses of GST-Src-SH2, GST-Src-SH2 + cortactin C112 and GST-Src-SH2 + cortactin C246 tryptic peptides

Journal: Journal of Cell Science

Article Title: Src binds cortactin through an SH2 domain cystine-mediated linkage

doi: 10.1242/jcs.121046

Figure Lengend Snippet: Observed and predicted ion masses of GST-Src-SH2, GST-Src-SH2 + cortactin C112 and GST-Src-SH2 + cortactin C246 tryptic peptides

Article Snippet: Screening of TransignalTM SH2 Domain Arrays (Panomics Cat. NO. MA3040) was conducted using 1.0 mg of each cortactin peptide according to the manufacturer's protocol.

Techniques:

Model of cysteine-mediated interactions in cortactin regulation. (A) Model of cysteine-based cortactin activation and phosphorylation by Src. (B) Phylogenetic co-conservation of cortactin C112/246 and Src C185. Conserved cysteines are in red and the homologous positions highlighted in yellow. (C) Cartoon representation of Src SH2 binding to phosphotyrosine and cysteine residues. Src amino acids 172–191 within the SH2 domain binding pocket are in white; interacting arginine 175 and cysteine 185 residues are in red. Cystine bonding is indicated as a red line. Phosphotyrosine and cystine binding ligands are listed. (D) Alignment of cysteine-containing SH2 domains. Domains known to bind ligands in a phosphotyrosine-independent manner are in bold italics. Cysteine residues are in red. Shading: green; hydrophobic, blue; positively charged, red; negatively charged, yellow; polar.

Journal: Journal of Cell Science

Article Title: Src binds cortactin through an SH2 domain cystine-mediated linkage

doi: 10.1242/jcs.121046

Figure Lengend Snippet: Model of cysteine-mediated interactions in cortactin regulation. (A) Model of cysteine-based cortactin activation and phosphorylation by Src. (B) Phylogenetic co-conservation of cortactin C112/246 and Src C185. Conserved cysteines are in red and the homologous positions highlighted in yellow. (C) Cartoon representation of Src SH2 binding to phosphotyrosine and cysteine residues. Src amino acids 172–191 within the SH2 domain binding pocket are in white; interacting arginine 175 and cysteine 185 residues are in red. Cystine bonding is indicated as a red line. Phosphotyrosine and cystine binding ligands are listed. (D) Alignment of cysteine-containing SH2 domains. Domains known to bind ligands in a phosphotyrosine-independent manner are in bold italics. Cysteine residues are in red. Shading: green; hydrophobic, blue; positively charged, red; negatively charged, yellow; polar.

Article Snippet: Screening of TransignalTM SH2 Domain Arrays (Panomics Cat. NO. MA3040) was conducted using 1.0 mg of each cortactin peptide according to the manufacturer's protocol.

Techniques: Activation Assay, Phospho-proteomics, Binding Assay

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