<p>Colored residues show the position of Zn-ligands (blue) and GSH-ligands (magenta). The transparent blue cone placed in the upper monomer mimics the general position of a ligand in the barrel containing the active site. The flexible loop that closes upon ligation over the barrel is colored in gold, the cysteine residues in shades of red. We suggest that covalent binding of GSH to Cys<sup>139</sup> brings about a conformational change to the flexible loop that might subsequently close the barrel.</p
To understand the dynamics of conformational changes during G protein activation, surface exposed cy...
<p>(A) Ligand structures after equilibration: antagonist (yellow) and agonist (purple). Helices repr...
<p>(a) The superposition of Cα traces of SigW/RsiW<sub>cyto</sub><sup>Red/Zn2+</sup> (zinc binding c...
<p>The 3D<b>-</b>EP24.15 structure focusing S-glutathiolated Cys residues is represented by ribbons ...
<p>The 3D<b>-</b>EP24.15 structure focusing S-glutathiolated Cys residues is surface represented and...
<p>18 representative conformations are shown (see supporting information II-IV; blue: flexible loop ...
<p>Superposition of CysC•ADP•APS (orange) and CysC•AMP-PNP•APS (green) on CysC•ADP (blue). Cys556 is...
<p>(A) Ribbon representation of monomer A with the GSH–CBL adduct atoms shown as van der Waals spher...
<p>This structual GPR83 homology model is based on the crystal structure of rhodopsin in the inactiv...
G-protein-coupled receptors (GPCRs) constitute the largest family of membrane receptors in eukaryote...
<p>(<b>A</b>) GST catalyzes the conjugation of PEITC with GSH in both forward (formation of GS-PEITC...
<p>The binding pocket is defined by those residues that have at least one heavy atom with a distance...
<p>Stereo view of the active site region, with molecule A (magenta) superimposed on to molecule B (l...
<p>Monomers are shown as ribbons, ligands as van der Waals surfaces. (A) Squid sigma-class GST with ...
<p>(A) Citric acid. (B) AMP-PNP. The auxiliary domain (colored yellow) is in the closed conformation...
To understand the dynamics of conformational changes during G protein activation, surface exposed cy...
<p>(A) Ligand structures after equilibration: antagonist (yellow) and agonist (purple). Helices repr...
<p>(a) The superposition of Cα traces of SigW/RsiW<sub>cyto</sub><sup>Red/Zn2+</sup> (zinc binding c...
<p>The 3D<b>-</b>EP24.15 structure focusing S-glutathiolated Cys residues is represented by ribbons ...
<p>The 3D<b>-</b>EP24.15 structure focusing S-glutathiolated Cys residues is surface represented and...
<p>18 representative conformations are shown (see supporting information II-IV; blue: flexible loop ...
<p>Superposition of CysC•ADP•APS (orange) and CysC•AMP-PNP•APS (green) on CysC•ADP (blue). Cys556 is...
<p>(A) Ribbon representation of monomer A with the GSH–CBL adduct atoms shown as van der Waals spher...
<p>This structual GPR83 homology model is based on the crystal structure of rhodopsin in the inactiv...
G-protein-coupled receptors (GPCRs) constitute the largest family of membrane receptors in eukaryote...
<p>(<b>A</b>) GST catalyzes the conjugation of PEITC with GSH in both forward (formation of GS-PEITC...
<p>The binding pocket is defined by those residues that have at least one heavy atom with a distance...
<p>Stereo view of the active site region, with molecule A (magenta) superimposed on to molecule B (l...
<p>Monomers are shown as ribbons, ligands as van der Waals surfaces. (A) Squid sigma-class GST with ...
<p>(A) Citric acid. (B) AMP-PNP. The auxiliary domain (colored yellow) is in the closed conformation...
To understand the dynamics of conformational changes during G protein activation, surface exposed cy...
<p>(A) Ligand structures after equilibration: antagonist (yellow) and agonist (purple). Helices repr...
<p>(a) The superposition of Cα traces of SigW/RsiW<sub>cyto</sub><sup>Red/Zn2+</sup> (zinc binding c...