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6vx6

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bestrophin-2 Ca2+-bound state (250 nM Ca2+)

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Retrieved from "http://52.214.119.220/wiki/index.php/6vx6"

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 <StructureSection load='6vx6' size='340' side='right'caption='[[6vx6]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6vx6]] 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=6VX6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6VX6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6vx6]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VX6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VX6 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=6vx6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vx6 OCA], [http://pdbe.org/6vx6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vx6 RCSB], [http://www.ebi.ac.uk/pdbsum/6vx6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vx6 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=6vx6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vx6 OCA], [https://pdbe.org/6vx6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vx6 RCSB], [https://www.ebi.ac.uk/pdbsum/6vx6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vx6 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/E1BF86_BOVIN E1BF86_BOVIN]] Forms calcium-sensitive chloride channels. Permeable to bicarbonate.[RuleBase:RU363126]
+[https://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>
+==See Also==
+*[[Bestrophin 3D structures|Bestrophin 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 6vx6" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Bovin]]
+[[Category: Bos taurus]]
 [[Category: Large Structures]]
-[[Category: Clarke, O]]
+[[Category: Clarke O]]
-[[Category: Fu, Z]]
+[[Category: Fu Z]]
-[[Category: Hendrickson, W A]]
+[[Category: Hendrickson WA]]
-[[Category: Hopiavuori, A]]
+[[Category: Hopiavuori A]]
-[[Category: Ji, C]]
+[[Category: Ji C]]
-[[Category: Kittredge, A]]
+[[Category: Kittredge A]]
-[[Category: Owji, A P]]
+[[Category: Owji AP]]
-[[Category: Shen, Y]]
+[[Category: Shen Y]]
-[[Category: Ward, N]]
+[[Category: Ward N]]
-[[Category: Yang, T]]
+[[Category: Yang T]]
-[[Category: Zhang, Y]]
+[[Category: Zhang Y]]
-[[Category: Zhao, Q]]
+[[Category: Zhao Q]]
-[[Category: Chloride channel]]
-[[Category: Membrane protein]]

6vx6

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Current revision

bestrophin-2 Ca2+-bound state (250 nM Ca2+)

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