Fifteen monomers form each one of the structures, and in both cases one monomer is colored in orange. The S-domain of the same monomer is indicated in red. (Right) Surface potentials of ExeD and EpsD, where blue and red colors represent basic and acidic residues, respectively. The membrane-binding region, in addition to a hydrophobic belt (white), also displays an acidic region formed mostly by residues from the S domain. In both cases, due to high flexibility in the N-terminal region, fitting was guided by the GspD models [11].</p
AbstractRhodopsin is the only member of the pharmacologically important superfamily of G-protein-cou...
<p>Isosurfaces of probe densities with grid free energy values ≤ -1 kcal/mol are shown in solution (...
<p>SMD, sub-membrane domain. Hydrophobic residues are in bold-face type. Positively charged residues...
<p>The F-BAR domain is shown as the all-atom (A) and the SBCG (B) model in side-view and top-view, w...
(A) EpsS is a compact molecule consisting of a 5-stranded antiparallel sheet buttressed by four majo...
<p>Their active site architecture is shown as surface with amino acid residues represented as lines ...
<p>(A) Electrostatic surface of the HADDOCK model with the docked diC6-PtdIns(4)P shown in sticks. (...
<p>Shown are reproducible EPR spectral overlays for the MTSSL spin-labeled GRP1 PH domain V278R1, il...
AbstractEpsin possesses a conserved epsin N-terminal homology (ENTH) domain that acts as a phosphati...
The N0 domain (Pfam domain family PF07660) is in cyan, the N1 and N1-like domains (PF03958) are in b...
<p>(<b>A</b>) The different ligands (sulfate (violet), phosphoserine (salmon), Ins(4)P (green) and a...
<p>On the left is a ribbon diagram of the model colored as a rainbow spectrum starting with red at t...
<p>The predicted structures of the first (A), second (B), third (C), and fourth (D) PDZ domain of Sj...
<p>(A) Model reconstructions of PgdS in solution. Right: <i>ab initio</i> models from DAMMIF model; ...
<p>Superposition of 1r1h (cyan), NEPv (yellow) and 2yb9 (violet), illustrating flexibility of size a...
AbstractRhodopsin is the only member of the pharmacologically important superfamily of G-protein-cou...
<p>Isosurfaces of probe densities with grid free energy values ≤ -1 kcal/mol are shown in solution (...
<p>SMD, sub-membrane domain. Hydrophobic residues are in bold-face type. Positively charged residues...
<p>The F-BAR domain is shown as the all-atom (A) and the SBCG (B) model in side-view and top-view, w...
(A) EpsS is a compact molecule consisting of a 5-stranded antiparallel sheet buttressed by four majo...
<p>Their active site architecture is shown as surface with amino acid residues represented as lines ...
<p>(A) Electrostatic surface of the HADDOCK model with the docked diC6-PtdIns(4)P shown in sticks. (...
<p>Shown are reproducible EPR spectral overlays for the MTSSL spin-labeled GRP1 PH domain V278R1, il...
AbstractEpsin possesses a conserved epsin N-terminal homology (ENTH) domain that acts as a phosphati...
The N0 domain (Pfam domain family PF07660) is in cyan, the N1 and N1-like domains (PF03958) are in b...
<p>(<b>A</b>) The different ligands (sulfate (violet), phosphoserine (salmon), Ins(4)P (green) and a...
<p>On the left is a ribbon diagram of the model colored as a rainbow spectrum starting with red at t...
<p>The predicted structures of the first (A), second (B), third (C), and fourth (D) PDZ domain of Sj...
<p>(A) Model reconstructions of PgdS in solution. Right: <i>ab initio</i> models from DAMMIF model; ...
<p>Superposition of 1r1h (cyan), NEPv (yellow) and 2yb9 (violet), illustrating flexibility of size a...
AbstractRhodopsin is the only member of the pharmacologically important superfamily of G-protein-cou...
<p>Isosurfaces of probe densities with grid free energy values ≤ -1 kcal/mol are shown in solution (...
<p>SMD, sub-membrane domain. Hydrophobic residues are in bold-face type. Positively charged residues...