View source for 5x87


==Crystal structure of a bacterial Bestrophin homolog from Klebsiella pneumoniae with a mutation L177T==
<StructureSection load='5x87' size='340' side='right'caption='[[5x87]], [[Resolution|resolution]] 3.14&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5x87]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X87 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5X87 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.14&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=5x87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x87 OCA], [https://pdbe.org/5x87 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5x87 RCSB], [https://www.ebi.ac.uk/pdbsum/5x87 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5x87 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/W1ELP7_KLEPN W1ELP7_KLEPN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mutations in the human BEST1 gene lead to retinal degenerative diseases displaying progressive vision loss and even blindness. BESTROPHIN1, encoded by BEST1, is predominantly expressed in retinal pigment epithelium (RPE), but its physiological role has been a mystery for the last two decades. Using a patient-specific iPSC-based disease model and interdisciplinary approaches, we comprehensively analyzed two distinct BEST1 patient mutations, and discovered mechanistic correlations between patient clinical phenotypes, electrophysiology in their RPEs, and the structure and function of BESTROPHIN1 mutant channels. Our results revealed that the disease-causing mechanism of BEST1 mutations is centered on the indispensable role of BESTROPHIN1 in mediating the long speculated Ca2+-dependent Cl- current in RPE, and demonstrate that the pathological potential of BEST1 mutations can be evaluated and predicted with our iPSC-based 'disease-in-a-dish' approach. Moreover, we demonstrated that patient RPE is rescuable with viral gene supplementation, providing a proof-of-concept for curing BEST1-associated diseases.

Patient-specific mutations impair BESTROPHIN1's essential role in mediating Ca2+-dependent Cl- currents in human RPE.,Li Y, Zhang Y, Xu Y, Kittredge A, Ward N, Chen S, Tsang SH, Yang T Elife. 2017 Oct 24;6. pii: e29914. doi: 10.7554/eLife.29914. PMID:29063836<ref>PMID:29063836</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5x87" style="background-color:#fffaf0;"></div>

==See Also==
*[[Bestrophin 3D structures|Bestrophin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Klebsiella pneumoniae]]
[[Category: Large Structures]]
[[Category: Chen S]]
[[Category: Yang T]]
[[Category: Zhang Y]]