5zsu
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Structure of protein== | |
| - | + | <StructureSection load='5zsu' size='340' side='right' caption='[[5zsu]], [[Resolution|resolution]] 4.25Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5zsu]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZSU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZSU FirstGlance]. <br> | |
| - | + | </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=5zsu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zsu OCA], [http://pdbe.org/5zsu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zsu RCSB], [http://www.ebi.ac.uk/pdbsum/5zsu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zsu ProSAT]</span></td></tr> | |
| - | [[Category: | + | </table> |
| + | == Disease == | ||
| + | [[http://www.uniprot.org/uniprot/LRC8A_HUMAN LRC8A_HUMAN]] Autosomal agammaglobulinemia. The disease is caused by mutations affecting the gene represented in this entry. A chromosomal aberration involving LRRC8 has been found in a patient with congenital agammaglobulinemia. Translocation t(9;20)(q33.2;q12). The translocation truncates the LRRC8 gene, resulting in deletion of the eighth, ninth, and half of the seventh LRR domains. | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/LRC8A_HUMAN LRC8A_HUMAN]] Essential component of the volume-regulated anion channel (VRAC, also named VSOAC channel), an anion channel required to maintain a constant cell volume in response to extracellular or intracellular osmotic changes (PubMed:24725410, PubMed:24790029, PubMed:26530471, PubMed:26824658, PubMed:28193731, PubMed:29769723). The VRAC channel conducts iodide better than chloride and can also conduct organic osmolytes like taurine (PubMed:24725410, PubMed:24790029, PubMed:26530471, PubMed:26824658, PubMed:28193731). Mediates efflux of amino acids, such as aspartate and glutamate, in response to osmotic stress (PubMed:28193731). LRRC8A and LRRC8D are required for the uptake of the drug cisplatin (PubMed:26530471). Required for in vivo channel activity, together with at least one other family member (LRRC8B, LRRC8C, LRRC8D or LRRC8E); channel characteristics depend on the precise subunit composition (PubMed:24790029, PubMed:26824658, PubMed:28193731). Can form functional channels by itself (in vitro) (PubMed:26824658). Involved in B-cell development: required for the pro-B cell to pre-B cell transition (PubMed:14660746). Also required for T-cell development (By similarity).[UniProtKB:Q80WG5]<ref>PMID:14660746</ref> <ref>PMID:24725410</ref> <ref>PMID:24790029</ref> <ref>PMID:26530471</ref> <ref>PMID:26824658</ref> <ref>PMID:28193731</ref> <ref>PMID:29769723</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Ishitani, R]] | ||
| + | [[Category: Kasuya, G]] | ||
| + | [[Category: Nakane, T]] | ||
| + | [[Category: Nureki, O]] | ||
| + | [[Category: Shirouzu, M]] | ||
| + | [[Category: Yokoyama, T]] | ||
| + | [[Category: Membrane protein]] | ||
Revision as of 16:09, 15 August 2018
Structure of protein
| |||||||||||
