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| | ==Cryo-EM structure of human CALHM2== | | ==Cryo-EM structure of human CALHM2== |
| - | <StructureSection load='6vak' size='340' side='right'caption='[[6vak]], [[Resolution|resolution]] 3.48Å' scene=''> | + | <SX load='6vak' size='340' side='right' viewer='molstar' caption='[[6vak]], [[Resolution|resolution]] 3.48Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6vak]] is a 11 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VAK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6VAK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6vak]] is a 11 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=6VAK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VAK FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CALHM2, FAM26B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.48Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6vak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vak OCA], [http://pdbe.org/6vak PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vak RCSB], [http://www.ebi.ac.uk/pdbsum/6vak PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vak ProSAT]</span></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=6vak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vak OCA], [https://pdbe.org/6vak PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vak RCSB], [https://www.ebi.ac.uk/pdbsum/6vak PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vak ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CAHM2_HUMAN CAHM2_HUMAN]] Pore-forming subunit of a voltage-gated ion channel.[UniProtKB:Q8IU99] | + | [https://www.uniprot.org/uniprot/CAHM2_HUMAN CAHM2_HUMAN] Pore-forming subunit of a voltage-gated ion channel.[UniProtKB:Q8IU99] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| - | </StructureSection> | + | </SX> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chou, T H]] | + | [[Category: Chou TH]] |
| - | [[Category: Furukawa, H]] | + | [[Category: Furukawa H]] |
| - | [[Category: Syrjanen, J L]] | + | [[Category: Syrjanen JL]] |
| - | [[Category: Assembly]]
| + | |
| - | [[Category: Membrane protein]]
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| - | [[Category: Taste]]
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| Structural highlights
Function
CAHM2_HUMAN Pore-forming subunit of a voltage-gated ion channel.[UniProtKB:Q8IU99]
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Syrjanen JL, Michalski K, Chou TH, Grant T, Rao S, Simorowski N, Tucker SJ, Grigorieff N, Furukawa H. Structure and assembly of calcium homeostasis modulator proteins. Nat Struct Mol Biol. 2020 Feb;27(2):150-159. doi: 10.1038/s41594-019-0369-9. Epub, 2020 Jan 27. PMID:31988524 doi:http://dx.doi.org/10.1038/s41594-019-0369-9
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