4rdq
From Proteopedia
(Difference between revisions)
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<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=4rdq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rdq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rdq RCSB], [http://www.ebi.ac.uk/pdbsum/4rdq PDBsum]</span></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=4rdq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rdq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rdq RCSB], [http://www.ebi.ac.uk/pdbsum/4rdq PDBsum]</span></td></tr> | ||
</table> | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Bestrophin calcium-activated chloride channels (CaCCs) regulate the flow of chloride and other monovalent anions across cellular membranes in response to intracellular calcium (Ca(2+)) levels. Mutations in bestrophin 1 (BEST1) cause certain eye diseases. Here we present X-ray structures of chicken BEST1-Fab complexes, at 2.85 A resolution, with permeant anions and Ca(2+). Representing, to our knowledge, the first structure of a CaCC, the eukaryotic BEST1 channel, which recapitulates CaCC function in liposomes, is formed from a pentameric assembly of subunits. Ca(2+) binds to the channel's large cytosolic region. A single ion pore, approximately 95 A in length, is located along the central axis and contains at least 15 binding sites for anions. A hydrophobic neck within the pore probably forms the gate. Phenylalanine residues within it may coordinate permeating anions via anion-pi interactions. Conformational changes observed near the 'Ca(2+) clasp' hint at the mechanism of Ca(2+)-dependent gating. Disease-causing mutations are prevalent within the gating apparatus. | ||
+ | |||
+ | Structure and insights into the function of a Ca(2+)-activated Cl(-) channel.,Kane Dickson V, Pedi L, Long SB Nature. 2014 Dec 11;516(7530):213-8. doi: 10.1038/nature13913. Epub 2014 Oct 22. PMID:25337878<ref>PMID:25337878</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
- | [[Category: Dickson, V K | + | [[Category: Dickson, V K]] |
- | [[Category: Long, S B | + | [[Category: Long, S B]] |
- | [[Category: Pedi, L | + | [[Category: Pedi, L]] |
[[Category: Anion channel]] | [[Category: Anion channel]] | ||
[[Category: Cacc]] | [[Category: Cacc]] |
Revision as of 10:50, 24 December 2014
Calcium-activated chloride channel bestrophin-1, from chicken, in complex with Fab antibody fragments, chloride and calcium
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