6lyg: Difference between revisions

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'''Unreleased structure'''


The entry 6lyg is ON HOLD
==Cryo-EM structure of the calcium homeostasis modulator 1 channel==
<StructureSection load='6lyg' size='340' side='right'caption='[[6lyg]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LYG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LYG 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]] 3.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=6lyg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lyg OCA], [https://pdbe.org/6lyg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lyg RCSB], [https://www.ebi.ac.uk/pdbsum/6lyg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lyg ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Calcium homeostasis modulator 1 (CALHM1) is a voltage-gated ATP release channel that plays an important role in neural gustatory signaling and the pathogenesis of Alzheimer's disease. Here, we present a cryo-electron microscopy structure of full-length Ca(2+)-free CALHM1 from Danio rerio at an overall resolution of 3.1 A. Our structure reveals an octameric architecture with a wide pore diameter of ~20 A, presumably representing the active conformation. The overall structure is substantially different from that of the isoform CALHM2, which forms both undecameric hemichannels and gap junctions. The N-terminal small helix folds back to the pore and forms an antiparallel interaction with transmembrane helix 1. Structural analysis revealed that the extracellular loop 1 region within the dimer interface may contribute to oligomeric assembly. A positive potential belt inside the pore was identified that may modulate ion permeation. Our structure offers insights into the assembly and gating mechanism of the CALHM1 channel.


Authors:  
Cryo-EM structure of the calcium homeostasis modulator 1 channel.,Ren Y, Wen T, Xi Z, Li S, Lu J, Zhang X, Yang X, Shen Y Sci Adv. 2020 Jul 17;6(29):eaba8161. doi: 10.1126/sciadv.aba8161. eCollection, 2020 Jul. PMID:32832630<ref>PMID:32832630</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 6lyg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Ren Y]]
[[Category: Shen Y]]
[[Category: Yang X]]
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