View source for 29tc


==Cryo-EM structure of homo-hexameric hLRRC8A double mutation I2C/L402W==
<StructureSection load='29tc' size='340' side='right'caption='[[29tc]], [[Resolution|resolution]] 2.54&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[29tc]] is a 6 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=29TC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=29TC 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]] 2.54&#8491;</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=29tc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=29tc OCA], [https://pdbe.org/29tc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=29tc RCSB], [https://www.ebi.ac.uk/pdbsum/29tc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=29tc ProSAT]</span></td></tr>
</table>
== Disease ==
[https://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 ==
[https://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: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Bertelli S]]
[[Category: Dutzler R]]
[[Category: Klussendorf M]]
[[Category: Pusch M]]
[[Category: Stauber T]]
[[Category: Wang L]]