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==CALCIUM-ACTIVATED CHLORIDE CHANNEL BESTROPHIN-1, FROM CHICKEN, IN COMPLEX WITH FAB ANTIBODY FRAGMENTS, CHLORIDE AND CALCIUM==
 
<StructureSection load='4rdq' size='340' side='right' caption='[[4rdq]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
==Calcium-activated chloride channel bestrophin-1, from chicken, in complex with Fab antibody fragments, chloride and calcium==
<StructureSection load='4rdq' size='340' side='right'caption='[[4rdq]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4rdq]] is a 15 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RDQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RDQ FirstGlance]. <br>
<table><tr><td colspan='2'>[[4rdq]] is a 15 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RDQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RDQ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C6N:6-CYCLOHEXYL-2-(4-CYCLOHEXYLBUTYL)-2-({[4-O-(ALPHA-D-GLUCOPYRANOSYL)-BETA-D-GLUCOPYRANOSYL]OXY}METHYL)HEXYL+4-O-ALPHA-D-GLUCOPYRANOSYL-BETA-D-GLUCOPYRANOSIDE'>C6N</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.85&#8491;</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>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C6N:6-CYCLOHEXYL-2-(4-CYCLOHEXYLBUTYL)-2-({[4-O-(ALPHA-D-GLUCOPYRANOSYL)-BETA-D-GLUCOPYRANOSYL]OXY}METHYL)HEXYL+4-O-ALPHA-D-GLUCOPYRANOSYL-BETA-D-GLUCOPYRANOSIDE'>C6N</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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=4rdq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rdq OCA], [https://pdbe.org/4rdq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rdq RCSB], [https://www.ebi.ac.uk/pdbsum/4rdq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rdq ProSAT]</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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4rdq" style="background-color:#fffaf0;"></div>
==See Also==
*[[Antibody 3D structures|Antibody 3D structures]]
*[[Bestrophin 3D structures|Bestrophin 3D structures]]
*[[3D structures of non-human antibody|3D structures of non-human antibody]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Dickson, V K.]]
[[Category: Dickson VK]]
[[Category: Long, S B.]]
[[Category: Long SB]]
[[Category: Pedi, L.]]
[[Category: Pedi L]]
[[Category: Anion channel]]
[[Category: Cacc]]
[[Category: Calcium-activated chloride channel]]
[[Category: Ion channel]]
[[Category: Membrane]]
[[Category: Membrane protein]]
[[Category: Transmembrane protein]]
[[Category: Transport protein]]