8d1j: Difference between revisions

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'''Unreleased structure'''


The entry 8d1j is ON HOLD until Paper Publication
==hBest1 5mM Ca2+ (Ca2+-bound) closed state==
<StructureSection load='8d1j' size='340' side='right'caption='[[8d1j]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8d1j]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8D1J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8D1J FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.05&#8491;</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=MC3:1,2-DIMYRISTOYL-RAC-GLYCERO-3-PHOSPHOCHOLINE'>MC3</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=8d1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8d1j OCA], [https://pdbe.org/8d1j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8d1j RCSB], [https://www.ebi.ac.uk/pdbsum/8d1j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8d1j ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/BEST1_HUMAN BEST1_HUMAN] Nanophthalmos;Adult-onset foveomacular vitelliform dystrophy;Best vitelliform macular dystrophy;MRCS syndrome;Autosomal recessive bestrophinopathy;Autosomal dominant vitreoretinochoroidopathy;Retinitis pigmentosa. The disease is caused by variants affecting the gene represented in this entry.  The disease is caused by variants affecting the gene represented in this entry.  The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry.
== Function ==
[https://www.uniprot.org/uniprot/BEST1_HUMAN BEST1_HUMAN] Forms calcium-sensitive chloride channels. Highly permeable to bicarbonate.<ref>PMID:11904445</ref> <ref>PMID:12907679</ref> <ref>PMID:18400985</ref>


Authors:  
==See Also==
 
*[[Bestrophin 3D structures|Bestrophin 3D structures]]
Description:  
== References ==
[[Category: Unreleased Structures]]
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Hendrickson WA]]
[[Category: Kittredge A]]
[[Category: Owji AP]]
[[Category: Tingting Y]]

Latest revision as of 12:41, 14 February 2024

hBest1 5mM Ca2+ (Ca2+-bound) closed statehBest1 5mM Ca2+ (Ca2+-bound) closed state

Structural highlights

8d1j is a 5 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 2.05Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

BEST1_HUMAN Nanophthalmos;Adult-onset foveomacular vitelliform dystrophy;Best vitelliform macular dystrophy;MRCS syndrome;Autosomal recessive bestrophinopathy;Autosomal dominant vitreoretinochoroidopathy;Retinitis pigmentosa. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry.

Function

BEST1_HUMAN Forms calcium-sensitive chloride channels. Highly permeable to bicarbonate.[1] [2] [3]

See Also

References

  1. ↑ Sun H, Tsunenari T, Yau KW, Nathans J. The vitelliform macular dystrophy protein defines a new family of chloride channels. Proc Natl Acad Sci U S A. 2002 Mar 19;99(6):4008-13. doi: 10.1073/pnas.052692999. PMID:11904445 doi:http://dx.doi.org/10.1073/pnas.052692999
  2. ↑ Tsunenari T, Sun H, Williams J, Cahill H, Smallwood P, Yau KW, Nathans J. Structure-function analysis of the bestrophin family of anion channels. J Biol Chem. 2003 Oct 17;278(42):41114-25. doi: 10.1074/jbc.M306150200. Epub 2003, Aug 7. PMID:12907679 doi:http://dx.doi.org/10.1074/jbc.M306150200
  3. ↑ Qu Z, Hartzell HC. Bestrophin Cl- channels are highly permeable to HCO3-. Am J Physiol Cell Physiol. 2008 Jun;294(6):C1371-7. doi:, 10.1152/ajpcell.00398.2007. Epub 2008 Apr 9. PMID:18400985 doi:http://dx.doi.org/10.1152/ajpcell.00398.2007

8d1j, resolution 2.05Å

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