<p>zNOD1-NACHT (A), zNOD2-NACHT (B) and mNLRC4-NACHT (C). The apo and holo conformations are shown as red and green respectively. The amino acids marked in blue are critical residues participate in ATP binding supported by experimental evidences, the residues marked in black may participate in ATP recognition have been proposed in this study and residues (Arg404 in zNOD2) didn’t form any interaction as compared to zNOD1.</p
(A) The mevalonate-bound MmMK active site, with mevalonate and MmMK residues in green, and (B) the 5...
Abstract Background One of the major challenges in post-genomic era is to provide functional annotat...
<p>(<b>A–F</b>) Summary of poses in various sampled conformations of zfP2<b>X</b>4. These conformati...
<p>The critical amino acids involved in ATP binding are highlighted in bold font.</p
<p>The protein is shown as cartoon; interacting amino acids are shown as lines and ATP as stick.9D) ...
<p>(A) Complex I for NOD1-NACHT, (B) Complex II for NOD1-NACHT, (C) Complex III for NOD1-NACHT, (D) ...
The critical ATP-binding residues (proved experimentally), presented in red-bold font; the residues ...
<p>Two panels show the position of affected residues (rotated 180°) at the interface between the LF ...
<p>A: Interdomain interactions extracted from the contact map difference ATP/ADP (see text for detai...
<p>A) The central structure of the main cluster of ATP-bound PaNTD and EcNTD were compared. The corr...
Binding mode of the compound (shown in yellow stick) and residues from ATP binding cavity from both ...
<p><b>A</b> Comparison of the CaMKI320-ATP complex with the apo CaMKI320. The CaMKI320-ATP complex i...
<p>The figure accompanies the distance of each observed H-bonds, specified electrostatic interaction...
<p>(A) Backbone-RMSD of zNOD1-NACHT, (B) Backbone-RMSD of zNOD2-NACHT, (C) Backbone-RMSD of mNLRC4-N...
<p><b>Copyright information:</b></p><p>Taken from "High-throughput identification of interacting pro...
(A) The mevalonate-bound MmMK active site, with mevalonate and MmMK residues in green, and (B) the 5...
Abstract Background One of the major challenges in post-genomic era is to provide functional annotat...
<p>(<b>A–F</b>) Summary of poses in various sampled conformations of zfP2<b>X</b>4. These conformati...
<p>The critical amino acids involved in ATP binding are highlighted in bold font.</p
<p>The protein is shown as cartoon; interacting amino acids are shown as lines and ATP as stick.9D) ...
<p>(A) Complex I for NOD1-NACHT, (B) Complex II for NOD1-NACHT, (C) Complex III for NOD1-NACHT, (D) ...
The critical ATP-binding residues (proved experimentally), presented in red-bold font; the residues ...
<p>Two panels show the position of affected residues (rotated 180°) at the interface between the LF ...
<p>A: Interdomain interactions extracted from the contact map difference ATP/ADP (see text for detai...
<p>A) The central structure of the main cluster of ATP-bound PaNTD and EcNTD were compared. The corr...
Binding mode of the compound (shown in yellow stick) and residues from ATP binding cavity from both ...
<p><b>A</b> Comparison of the CaMKI320-ATP complex with the apo CaMKI320. The CaMKI320-ATP complex i...
<p>The figure accompanies the distance of each observed H-bonds, specified electrostatic interaction...
<p>(A) Backbone-RMSD of zNOD1-NACHT, (B) Backbone-RMSD of zNOD2-NACHT, (C) Backbone-RMSD of mNLRC4-N...
<p><b>Copyright information:</b></p><p>Taken from "High-throughput identification of interacting pro...
(A) The mevalonate-bound MmMK active site, with mevalonate and MmMK residues in green, and (B) the 5...
Abstract Background One of the major challenges in post-genomic era is to provide functional annotat...
<p>(<b>A–F</b>) Summary of poses in various sampled conformations of zfP2<b>X</b>4. These conformati...