View source for 6vai


==Cryo-EM structure of a dimer of undecameric human CALHM2==
<SX load='6vai' size='340' side='right' viewer='molstar' caption='[[6vai]], [[Resolution|resolution]] 3.68&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6vai]] is a 22 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=6VAI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VAI 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]] 3.68&#8491;</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=6vai FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vai OCA], [https://pdbe.org/6vai PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vai RCSB], [https://www.ebi.ac.uk/pdbsum/6vai PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vai ProSAT]</span></td></tr>
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== Function ==
[https://www.uniprot.org/uniprot/CAHM2_HUMAN CAHM2_HUMAN] Pore-forming subunit of a voltage-gated ion channel.[UniProtKB:Q8IU99]
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== Publication Abstract from PubMed ==
The biological membranes of many cell types contain large-pore channels through which a wide variety of ions and metabolites permeate. Examples include connexin, innexin and pannexin, which form gap junctions and/or bona fide cell surface channels. The most recently identified large-pore channels are the calcium homeostasis modulators (CALHMs), through which ions and ATP permeate in a voltage-dependent manner to control neuronal excitability, taste signaling and pathologies of depression and Alzheimer's disease. Despite such critical biological roles, the structures and patterns of their oligomeric assembly remain unclear. Here, we reveal the structures of two CALHMs, chicken CALHM1 and human CALHM2, by single-particle cryo-electron microscopy (cryo-EM), which show novel assembly of the four transmembrane helices into channels of octamers and undecamers, respectively. Furthermore, molecular dynamics simulations suggest that lipids can favorably assemble into a bilayer within the larger CALHM2 pore, but not within CALHM1, demonstrating the potential correlation between pore size, lipid accommodation and channel activity.

Structure and assembly of calcium homeostasis modulator proteins.,Syrjanen JL, Michalski K, Chou TH, Grant T, Rao S, Simorowski N, Tucker SJ, Grigorieff N, Furukawa H Nat Struct Mol Biol. 2020 Feb;27(2):150-159. doi: 10.1038/s41594-019-0369-9. Epub, 2020 Jan 27. PMID:31988524<ref>PMID:31988524</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6vai" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Chou TH]]
[[Category: Furukawa H]]
[[Category: Syrjanen JL]]