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6vx8
From Proteopedia
(Difference between revisions)
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<StructureSection load='6vx8' size='340' side='right'caption='[[6vx8]], [[Resolution|resolution]] 2.33Å' scene=''> | <StructureSection load='6vx8' size='340' side='right'caption='[[6vx8]], [[Resolution|resolution]] 2.33Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6vx8]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VX8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6VX8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6vx8]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VX8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6VX8 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BEST2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6vx8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vx8 OCA], [http://pdbe.org/6vx8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vx8 RCSB], [http://www.ebi.ac.uk/pdbsum/6vx8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vx8 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6vx8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vx8 OCA], [http://pdbe.org/6vx8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vx8 RCSB], [http://www.ebi.ac.uk/pdbsum/6vx8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vx8 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/E1BF86_BOVIN E1BF86_BOVIN]] Forms calcium-sensitive chloride channels. Permeable to bicarbonate.[RuleBase:RU363126] | [[http://www.uniprot.org/uniprot/E1BF86_BOVIN E1BF86_BOVIN]] Forms calcium-sensitive chloride channels. Permeable to bicarbonate.[RuleBase:RU363126] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The bestrophin family of calcium (Ca(2+))-activated chloride (Cl(-)) channels, which mediate the influx and efflux of monovalent anions in response to the levels of intracellular Ca(2+), comprises four members in mammals (bestrophin 1-4). Here we report cryo-EM structures of bovine bestrophin-2 (bBest2) bound and unbound by Ca(2+) at 2.4- and 2.2-A resolution, respectively. The bBest2 structure highlights four previously underappreciated pore-lining residues specifically conserved in Best2 but not in Best1, illustrating the differences between these paralogs. Structure-inspired electrophysiological analysis reveals that, although the channel is sensitive to Ca(2+), it has substantial Ca(2+)-independent activity for Cl(-), reflecting the opening at the cytoplasmic restriction of the ion conducting pathway even when Ca(2+) is absent. Moreover, the ion selectivity of bBest2 is controlled by multiple residues, including those involved in gating. | ||
| + | |||
| + | Structural and functional characterization of the bestrophin-2 anion channel.,Owji AP, Zhao Q, Ji C, Kittredge A, Hopiavuori A, Fu Z, Ward N, Clarke OB, Shen Y, Zhang Y, Hendrickson WA, Yang T Nat Struct Mol Biol. 2020 Apr;27(4):382-391. doi: 10.1038/s41594-020-0402-z. Epub, 2020 Apr 6. PMID:32251414<ref>PMID:32251414</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6vx8" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Bovin]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Clarke, O]] | [[Category: Clarke, O]] | ||
Revision as of 06:13, 22 April 2020
bestrophin-2 Ca2+- unbound state 2 (EGTA only)
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Categories: Bovin | Large Structures | Clarke, O | Fu, Z | Hendrickson, W A | Hopiavuori, A | Ji, C | Kittredge, A | Owji, A P | Shen, Y | Ward, N | Yang, T | Zhang, Y | Zhao, Q | Chloride channel | Membrane protein
