<p>(A) Tip114-STAT3, (B) Tip127-STAT3, (C) Tip114-STAT6, and (D) Tip127-STAT6. For each complex, three panels are shown that highlight the interactions formed in region I, II, and III. The backbone topology of STAT is shown as cyan ribbon and the interacting residues are shown in ball-and-stick presentation. Tip those residues that bind to STAT are shown in stick presentation and labeled in italics. Polar interactions (hydrogen bonds, salt-bridges) are indicated as dotted red lines.</p
<p>The interacting residues forms hydrogen bond, hydrophobic, and cation- π interactions are listed....
Left column: visualization of the NS3-4A protease structure and surface of the binding pocket of wi...
<p>Detailed analysis of the interaction partners of the dimerization hot spots (i.e. amino acids inv...
<p>Only those interactions that were stable over more than 30% of the simulation time are reported. ...
<p>(A) Tip and STAT structural domains (not to scale). (Top) From amino-terminus to carboxy-terminus...
<p>FhCL3 residues interacting with Nitrile (A), HTS12701 (B), BTB03219 (C). Ligands (violet) and pro...
<p>Upper: the interaction map between caspase-3 and acteoside. Lower: the interaction map between ca...
There is a growing recognition for the importance of proteins with large intrinsically disordered (I...
<p>(A) WT; (B) Pmut. Pair mutation sites were shown with sticks: magenta represented L175 in WT and ...
<p>Residue coloring scheme is similar to <a href="http://www.plosone.org/article/info:doi/10.1371/jo...
<p>(A) Complex structure of Nbp35-Cfd1 where the molecular contacts are highlighted (blue–Nbp35) and...
<p>The top layer divides protein-ligand complexes into 5 major groups based on the type of the ligan...
<p>The interactions of FNC,3TC and DC with residues 214 and 160 of RT are shown. FNC, 3TC and DC are...
<p>Residues involved in the formation of H-bond are in bold while both bold and italic are involved ...
<p>a: synthetic small molecules bound to proteins; b: protein-protein interactions small molecule in...
<p>The interacting residues forms hydrogen bond, hydrophobic, and cation- π interactions are listed....
Left column: visualization of the NS3-4A protease structure and surface of the binding pocket of wi...
<p>Detailed analysis of the interaction partners of the dimerization hot spots (i.e. amino acids inv...
<p>Only those interactions that were stable over more than 30% of the simulation time are reported. ...
<p>(A) Tip and STAT structural domains (not to scale). (Top) From amino-terminus to carboxy-terminus...
<p>FhCL3 residues interacting with Nitrile (A), HTS12701 (B), BTB03219 (C). Ligands (violet) and pro...
<p>Upper: the interaction map between caspase-3 and acteoside. Lower: the interaction map between ca...
There is a growing recognition for the importance of proteins with large intrinsically disordered (I...
<p>(A) WT; (B) Pmut. Pair mutation sites were shown with sticks: magenta represented L175 in WT and ...
<p>Residue coloring scheme is similar to <a href="http://www.plosone.org/article/info:doi/10.1371/jo...
<p>(A) Complex structure of Nbp35-Cfd1 where the molecular contacts are highlighted (blue–Nbp35) and...
<p>The top layer divides protein-ligand complexes into 5 major groups based on the type of the ligan...
<p>The interactions of FNC,3TC and DC with residues 214 and 160 of RT are shown. FNC, 3TC and DC are...
<p>Residues involved in the formation of H-bond are in bold while both bold and italic are involved ...
<p>a: synthetic small molecules bound to proteins; b: protein-protein interactions small molecule in...
<p>The interacting residues forms hydrogen bond, hydrophobic, and cation- π interactions are listed....
Left column: visualization of the NS3-4A protease structure and surface of the binding pocket of wi...
<p>Detailed analysis of the interaction partners of the dimerization hot spots (i.e. amino acids inv...