8gmq
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Chicken CALHM1 purified from mammalian cells== | |
| + | <StructureSection load='8gmq' size='340' side='right'caption='[[8gmq]], [[Resolution|resolution]] 3.36Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8gmq]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8GMQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8GMQ 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]] 3.36Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=POV:(2S)-3-(HEXADECANOYLOXY)-2-[(9Z)-OCTADEC-9-ENOYLOXY]PROPYL+2-(TRIMETHYLAMMONIO)ETHYL+PHOSPHATE'>POV</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=8gmq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8gmq OCA], [https://pdbe.org/8gmq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8gmq RCSB], [https://www.ebi.ac.uk/pdbsum/8gmq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8gmq ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A8V0ZGE7_CHICK A0A8V0ZGE7_CHICK] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Calcium homeostasis modulator 1 (CALHM1) is a voltage-dependent channel involved in neuromodulation and gustatory signaling. Despite recent progress in the structural biology of CALHM1, insights into functional regulation, pore architecture, and channel blockade remain limited. Here we present the cryo-EM structure of human CALHM1, revealing an octameric assembly pattern similar to the non-mammalian CALHM1s and the lipid-binding pocket conserved across species. We demonstrate by MD simulations that this pocket preferentially binds a phospholipid over cholesterol to stabilize its structure and regulate the channel activities. Finally, we show that residues in the amino-terminal helix form the channel pore that ruthenium red binds and blocks. | ||
| - | + | Structure of human CALHM1 reveals key locations for channel regulation and blockade by ruthenium red.,Syrjanen JL, Epstein M, Gomez R, Furukawa H Nat Commun. 2023 Jun 28;14(1):3821. doi: 10.1038/s41467-023-39388-3. PMID:37380652<ref>PMID:37380652</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8gmq" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Gallus gallus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Furukawa H]] | ||
| + | [[Category: Syrjanen JL]] | ||
Current revision
Chicken CALHM1 purified from mammalian cells
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