8xmn: Difference between revisions
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==Voltage-gated sodium channel Nav1.7 variant M2== | |||
<StructureSection load='8xmn' size='340' side='right'caption='[[8xmn]], [[Resolution|resolution]] 3.37Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8xmn]] is a 3 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=8XMN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8XMN 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]] 3.37Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=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=8xmn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8xmn OCA], [https://pdbe.org/8xmn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8xmn RCSB], [https://www.ebi.ac.uk/pdbsum/8xmn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8xmn 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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8xmn" style="background-color:#fffaf0;"></div> | ||
[[Category: Huang | == References == | ||
[[Category: Li | <references/> | ||
[[Category: Wu | __TOC__ | ||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Huang G]] | |||
[[Category: Li Z]] | |||
[[Category: Wu Q]] | |||
[[Category: Yan N]] | |||