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6ivk
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of a membrane protein G175A== | |
| + | <StructureSection load='6ivk' size='340' side='right'caption='[[6ivk]], [[Resolution|resolution]] 2.65Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6ivk]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IVK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IVK FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=6ivk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ivk OCA], [http://pdbe.org/6ivk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ivk RCSB], [http://www.ebi.ac.uk/pdbsum/6ivk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ivk ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Mutations of human BEST1, encoding a Ca(2+)-activated Cl(-) channel (hBest1), cause macular degenerative disorders. Best1 homolog structures reveal an evolutionarily conserved channel architecture highlighted by two landmark restrictions (named the "neck" and "aperture", respectively) in the ion conducting pathway, suggesting a unique dual-switch gating mechanism, which, however, has not been characterized well. Using patch clamp and crystallography, we demonstrate that both the neck and aperture in hBest1 are Ca(2+)-dependent gates essential for preventing channel leakage resulting from Ca(2+)-independent, spontaneous gate opening. Importantly, three patient-derived mutations (D203A, I205T and Y236C) lead to Ca(2+)-independent leakage and elevated Ca(2+)-dependent anion currents due to enhanced opening of the gates. Moreover, we identify a network of residues critically involved in gate operation. Together, our results suggest an indispensable role of the neck and aperture of hBest1 for channel gating, and uncover disease-causing mechanisms of hBest1 gain-of-function mutations. | ||
| - | + | Dual Ca(2+)-dependent gates in human Bestrophin1 underlie disease-causing mechanisms of gain-of-function mutations.,Ji C, Kittredge A, Hopiavuori A, Ward N, Chen S, Fukuda Y, Zhang Y, Yang T Commun Biol. 2019 Jun 24;2:240. doi: 10.1038/s42003-019-0433-3. eCollection 2019. PMID:31263784<ref>PMID:31263784</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 6ivk" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Fukuda, F]] | [[Category: Fukuda, F]] | ||
| - | [[Category: | + | [[Category: Kittredge, A]] |
[[Category: Yang, T]] | [[Category: Yang, T]] | ||
| + | [[Category: Zhang, Y]] | ||
| + | [[Category: Membrane protein]] | ||
Revision as of 06:37, 6 November 2019
Crystal structure of a membrane protein G175A
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