8zsz
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==Cryo-EM structure of human ZnT1, in the presence of zinc, determined in outward-facing conformation== | |
- | + | <StructureSection load='8zsz' size='340' side='right'caption='[[8zsz]], [[Resolution|resolution]] 3.59Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[8zsz]] is a 2 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=8ZSZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ZSZ 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]] 3.59Å</td></tr> | |
- | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8zsz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8zsz OCA], [https://pdbe.org/8zsz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8zsz RCSB], [https://www.ebi.ac.uk/pdbsum/8zsz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8zsz ProSAT]</span></td></tr> |
- | [[Category: | + | </table> |
- | [[Category: Ma | + | == Function == |
+ | [https://www.uniprot.org/uniprot/ZNT1_HUMAN ZNT1_HUMAN] Zinc ion:proton antiporter that could function at the plasma membrane mediating zinc efflux from cells against its electrochemical gradient protecting them from intracellular zinc accumulation and toxicity (PubMed:31471319). Alternatively, could prevent the transport to the plasma membrane of CACNB2, the L-type calcium channels regulatory subunit, through a yet to be defined mechanism. By modulating the expression of these channels at the plasma membrane, could prevent calcium and zinc influx into cells. By the same mechanism, could also prevent L-type calcium channels-mediated heavy metal influx into cells (By similarity). In some cells, could also function as a zinc ion:proton antiporter mediating zinc entry into the lumen of cytoplasmic vesicles. In macrophages, can increase zinc ions concentration into the lumen of cytoplasmic vesicles containing engulfed bacteria and could help inactivate them (PubMed:32441444).[UniProtKB:Q62720]<ref>PMID:31471319</ref> <ref>PMID:32441444</ref> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Homo sapiens]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Ma J]] | ||
+ | [[Category: Zheng S]] |
Current revision
Cryo-EM structure of human ZnT1, in the presence of zinc, determined in outward-facing conformation
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