8xmm: Difference between revisions

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-'''Unreleased structure'''
-The entry 8xmm is ON HOLD
+==Voltage-gated sodium channel Nav1.7 variant M9==
+<StructureSection load='8xmm' size='340' side='right'caption='[[8xmm]], [[Resolution|resolution]] 2.89&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8xmm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8XMM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8XMM FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.89&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PW:(2S,3R,4E)-2-(ACETYLAMINO)-3-HYDROXYOCTADEC-4-EN-1-YL+DIHYDROGEN+PHOSPHATE'>1PW</scene>, <scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=LPE:1-O-OCTADECYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>LPE</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=P5S:O-[(R)-{[(2R)-2,3-BIS(OCTADECANOYLOXY)PROPYL]OXY}(HYDROXY)PHOSPHORYL]-L-SERINE'>P5S</scene>, <scene name='pdbligand=PCW:1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>PCW</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8xmm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8xmm OCA], [https://pdbe.org/8xmm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8xmm RCSB], [https://www.ebi.ac.uk/pdbsum/8xmm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8xmm ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Voltage-gated sodium channels (Na(v)) undergo conformational shifts in response to membrane potential changes, a mechanism known as the electromechanical coupling. To delineate the structure-function relationship of human Na(v) channels, we have performed systematic structural analysis using human Na(v)1.7 as a prototype. Guided by the structural differences between wild-type (WT) Na(v)1.7 and an eleven mutation-containing variant, designated Na(v)1.7-M11, we generated three additional intermediate mutants and solved their structures at overall resolutions of 2.9-3.4 A. The mutant with nine-point mutations in the pore domain (PD), named Na(v)1.7-M9, has a reduced cavity volume and a sealed gate, with all voltage-sensing domains (VSDs) remaining up. Structural comparison of WT and Na(v)1.7-M9 pinpoints two residues that may be critical to the tightening of the PD. However, the variant containing these two mutations, Na(v)1.7-M2, or even in combination with two additional mutations in the VSDs, named Na(v)1.7-M4, failed to tighten the PD. Our structural analysis reveals a tendency of PD contraction correlated with the right shift of the static inactivation I-V curves. We predict that the channel in the resting state should have a "tight" PD with down VSDs.
-Authors:
+Dissection of the structure-function relationship of Na(v) channels.,Li Z, Wu Q, Huang G, Jin X, Li J, Pan X, Yan N Proc Natl Acad Sci U S A. 2024 Feb 27;121(9):e2322899121. doi: , 10.1073/pnas.2322899121. Epub 2024 Feb 21. PMID:38381792<ref>PMID:38381792</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 8xmm" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Huang G]]
+[[Category: Li Z]]
+[[Category: Wu Q]]
+[[Category: Yan N]]