graphical modeling environment 78 Search Results


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3D structures of the RhoA, RhoB and RhoC G domain. (A–C) Ribbon representation of (A) RhoA (4–180 aa; Protein Data Bank (PDB) ID: 1FTN),75 (B) RhoB (4–185 aa; PDB ID: 2FV8)76 and (C) RhoC (3–179 aa; PDB ID: 2GCN).77 Structures are shown in the same orientation. Switch I, switch II and the insert region are highlighted in gray, GDP is shown in yellow sticks. Residues marked in cyan differ among RhoA/B/C (underlined labeling in A) and are different compared to Rac1/Cdc42 (labeling in C). (D–F) Zooms of A–C highlighting that RhoA and RhoB contain at position 43 a valine, whereas RhoC has an isoleucine which has slightly bulkier side chain which underlies isoform-specific GEF- and effector binding (see text). (G–I) Electrostatic potential of the solvent accessible surface of the G domains of (G) RhoA, (H) RhoB and (I) RhoC represented in the same orientation as in A–C, lower panels show cognate structures rotated by 180°. Note that the hypervariable C-termini are not included in this representation. Electrostatic potential was calculated using the Adaptive Poisson-Boltzmann Solver (APBS) software, combined with the PDB2PQR server, at a pH of 7.5 and a threshold of ± 5 kTe−1 (red – negative charge; blue – positive charge).78 Figures were prepared with <t>PyMol</t> <t>(PyMol</t> <t>Molecular</t> Graphics System, Schroedinger, LLC).
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3D structures of the RhoA, RhoB and RhoC G domain. (A–C) Ribbon representation of (A) RhoA (4–180 aa; Protein Data Bank (PDB) ID: 1FTN),75 (B) RhoB (4–185 aa; PDB ID: 2FV8)76 and (C) RhoC (3–179 aa; PDB ID: 2GCN).77 Structures are shown in the same orientation. Switch I, switch II and the insert region are highlighted in gray, GDP is shown in yellow sticks. Residues marked in cyan differ among RhoA/B/C (underlined labeling in A) and are different compared to Rac1/Cdc42 (labeling in C). (D–F) Zooms of A–C highlighting that RhoA and RhoB contain at position 43 a valine, whereas RhoC has an isoleucine which has slightly bulkier side chain which underlies isoform-specific GEF- and effector binding (see text). (G–I) Electrostatic potential of the solvent accessible surface of the G domains of (G) RhoA, (H) RhoB and (I) RhoC represented in the same orientation as in A–C, lower panels show cognate structures rotated by 180°. Note that the hypervariable C-termini are not included in this representation. Electrostatic potential was calculated using the Adaptive Poisson-Boltzmann Solver (APBS) software, combined with the PDB2PQR server, at a pH of 7.5 and a threshold of ± 5 kTe−1 (red – negative charge; blue – positive charge).78 Figures were prepared with <t>PyMol</t> <t>(PyMol</t> <t>Molecular</t> Graphics System, Schroedinger, LLC).
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3D structures of the RhoA, RhoB and RhoC G domain. (A–C) Ribbon representation of (A) RhoA (4–180 aa; Protein Data Bank (PDB) ID: 1FTN),75 (B) RhoB (4–185 aa; PDB ID: 2FV8)76 and (C) RhoC (3–179 aa; PDB ID: 2GCN).77 Structures are shown in the same orientation. Switch I, switch II and the insert region are highlighted in gray, GDP is shown in yellow sticks. Residues marked in cyan differ among RhoA/B/C (underlined labeling in A) and are different compared to Rac1/Cdc42 (labeling in C). (D–F) Zooms of A–C highlighting that RhoA and RhoB contain at position 43 a valine, whereas RhoC has an isoleucine which has slightly bulkier side chain which underlies isoform-specific GEF- and effector binding (see text). (G–I) Electrostatic potential of the solvent accessible surface of the G domains of (G) RhoA, (H) RhoB and (I) RhoC represented in the same orientation as in A–C, lower panels show cognate structures rotated by 180°. Note that the hypervariable C-termini are not included in this representation. Electrostatic potential was calculated using the Adaptive Poisson-Boltzmann Solver (APBS) software, combined with the PDB2PQR server, at a pH of 7.5 and a threshold of ± 5 kTe−1 (red – negative charge; blue – positive charge).78 Figures were prepared with <t>PyMol</t> <t>(PyMol</t> <t>Molecular</t> Graphics System, Schroedinger, LLC).
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3D structures of the RhoA, RhoB and RhoC G domain. (A–C) Ribbon representation of (A) RhoA (4–180 aa; Protein Data Bank (PDB) ID: 1FTN),75 (B) RhoB (4–185 aa; PDB ID: 2FV8)76 and (C) RhoC (3–179 aa; PDB ID: 2GCN).77 Structures are shown in the same orientation. Switch I, switch II and the insert region are highlighted in gray, GDP is shown in yellow sticks. Residues marked in cyan differ among RhoA/B/C (underlined labeling in A) and are different compared to Rac1/Cdc42 (labeling in C). (D–F) Zooms of A–C highlighting that RhoA and RhoB contain at position 43 a valine, whereas RhoC has an isoleucine which has slightly bulkier side chain which underlies isoform-specific GEF- and effector binding (see text). (G–I) Electrostatic potential of the solvent accessible surface of the G domains of (G) RhoA, (H) RhoB and (I) RhoC represented in the same orientation as in A–C, lower panels show cognate structures rotated by 180°. Note that the hypervariable C-termini are not included in this representation. Electrostatic potential was calculated using the Adaptive Poisson-Boltzmann Solver (APBS) software, combined with the PDB2PQR server, at a pH of 7.5 and a threshold of ± 5 kTe−1 (red – negative charge; blue – positive charge).78 Figures were prepared with <t>PyMol</t> <t>(PyMol</t> <t>Molecular</t> Graphics System, Schroedinger, LLC).
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3D structures of the RhoA, RhoB and RhoC G domain. (A–C) Ribbon representation of (A) RhoA (4–180 aa; Protein Data Bank (PDB) ID: 1FTN),75 (B) RhoB (4–185 aa; PDB ID: 2FV8)76 and (C) RhoC (3–179 aa; PDB ID: 2GCN).77 Structures are shown in the same orientation. Switch I, switch II and the insert region are highlighted in gray, GDP is shown in yellow sticks. Residues marked in cyan differ among RhoA/B/C (underlined labeling in A) and are different compared to Rac1/Cdc42 (labeling in C). (D–F) Zooms of A–C highlighting that RhoA and RhoB contain at position 43 a valine, whereas RhoC has an isoleucine which has slightly bulkier side chain which underlies isoform-specific GEF- and effector binding (see text). (G–I) Electrostatic potential of the solvent accessible surface of the G domains of (G) RhoA, (H) RhoB and (I) RhoC represented in the same orientation as in A–C, lower panels show cognate structures rotated by 180°. Note that the hypervariable C-termini are not included in this representation. Electrostatic potential was calculated using the Adaptive Poisson-Boltzmann Solver (APBS) software, combined with the PDB2PQR server, at a pH of 7.5 and a threshold of ± 5 kTe−1 (red – negative charge; blue – positive charge).78 Figures were prepared with <t>PyMol</t> <t>(PyMol</t> <t>Molecular</t> Graphics System, Schroedinger, LLC).
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3D structures of the RhoA, RhoB and RhoC G domain. (A–C) Ribbon representation of (A) RhoA (4–180 aa; Protein Data Bank (PDB) ID: 1FTN),75 (B) RhoB (4–185 aa; PDB ID: 2FV8)76 and (C) RhoC (3–179 aa; PDB ID: 2GCN).77 Structures are shown in the same orientation. Switch I, switch II and the insert region are highlighted in gray, GDP is shown in yellow sticks. Residues marked in cyan differ among RhoA/B/C (underlined labeling in A) and are different compared to Rac1/Cdc42 (labeling in C). (D–F) Zooms of A–C highlighting that RhoA and RhoB contain at position 43 a valine, whereas RhoC has an isoleucine which has slightly bulkier side chain which underlies isoform-specific GEF- and effector binding (see text). (G–I) Electrostatic potential of the solvent accessible surface of the G domains of (G) RhoA, (H) RhoB and (I) RhoC represented in the same orientation as in A–C, lower panels show cognate structures rotated by 180°. Note that the hypervariable C-termini are not included in this representation. Electrostatic potential was calculated using the Adaptive Poisson-Boltzmann Solver (APBS) software, combined with the PDB2PQR server, at a pH of 7.5 and a threshold of ± 5 kTe−1 (red – negative charge; blue – positive charge).78 Figures were prepared with <t>PyMol</t> <t>(PyMol</t> <t>Molecular</t> Graphics System, Schroedinger, LLC).
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Image Search Results


3D structures of the RhoA, RhoB and RhoC G domain. (A–C) Ribbon representation of (A) RhoA (4–180 aa; Protein Data Bank (PDB) ID: 1FTN),75 (B) RhoB (4–185 aa; PDB ID: 2FV8)76 and (C) RhoC (3–179 aa; PDB ID: 2GCN).77 Structures are shown in the same orientation. Switch I, switch II and the insert region are highlighted in gray, GDP is shown in yellow sticks. Residues marked in cyan differ among RhoA/B/C (underlined labeling in A) and are different compared to Rac1/Cdc42 (labeling in C). (D–F) Zooms of A–C highlighting that RhoA and RhoB contain at position 43 a valine, whereas RhoC has an isoleucine which has slightly bulkier side chain which underlies isoform-specific GEF- and effector binding (see text). (G–I) Electrostatic potential of the solvent accessible surface of the G domains of (G) RhoA, (H) RhoB and (I) RhoC represented in the same orientation as in A–C, lower panels show cognate structures rotated by 180°. Note that the hypervariable C-termini are not included in this representation. Electrostatic potential was calculated using the Adaptive Poisson-Boltzmann Solver (APBS) software, combined with the PDB2PQR server, at a pH of 7.5 and a threshold of ± 5 kTe−1 (red – negative charge; blue – positive charge).78 Figures were prepared with PyMol (PyMol Molecular Graphics System, Schroedinger, LLC).

Journal: Small GTPases

Article Title: Toward understanding RhoGTPase specificity: structure, function and local activation

doi: 10.4161/21541248.2014.968004

Figure Lengend Snippet: 3D structures of the RhoA, RhoB and RhoC G domain. (A–C) Ribbon representation of (A) RhoA (4–180 aa; Protein Data Bank (PDB) ID: 1FTN),75 (B) RhoB (4–185 aa; PDB ID: 2FV8)76 and (C) RhoC (3–179 aa; PDB ID: 2GCN).77 Structures are shown in the same orientation. Switch I, switch II and the insert region are highlighted in gray, GDP is shown in yellow sticks. Residues marked in cyan differ among RhoA/B/C (underlined labeling in A) and are different compared to Rac1/Cdc42 (labeling in C). (D–F) Zooms of A–C highlighting that RhoA and RhoB contain at position 43 a valine, whereas RhoC has an isoleucine which has slightly bulkier side chain which underlies isoform-specific GEF- and effector binding (see text). (G–I) Electrostatic potential of the solvent accessible surface of the G domains of (G) RhoA, (H) RhoB and (I) RhoC represented in the same orientation as in A–C, lower panels show cognate structures rotated by 180°. Note that the hypervariable C-termini are not included in this representation. Electrostatic potential was calculated using the Adaptive Poisson-Boltzmann Solver (APBS) software, combined with the PDB2PQR server, at a pH of 7.5 and a threshold of ± 5 kTe−1 (red – negative charge; blue – positive charge).78 Figures were prepared with PyMol (PyMol Molecular Graphics System, Schroedinger, LLC).

Article Snippet: 78 Figures were prepared with PyMol (PyMol Molecular Graphics System, Schroedinger, LLC).

Techniques: Labeling, Binding Assay, Solvent, Software