5v3r
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==CHMP4C in complex with ALIX BRO1== | |
- | + | <StructureSection load='5v3r' size='340' side='right' caption='[[5v3r]], [[Resolution|resolution]] 1.91Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[5v3r]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V3R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5V3R FirstGlance]. <br> | |
- | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3c3r|3c3r]], [[5v3k|5v3k]]</td></tr> | |
- | [[Category: | + | <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=5v3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v3r OCA], [http://pdbe.org/5v3r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5v3r RCSB], [http://www.ebi.ac.uk/pdbsum/5v3r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5v3r ProSAT]</span></td></tr> |
+ | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/PDC6I_HUMAN PDC6I_HUMAN]] Class E VPS protein involved in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome. Binds to the phospholipid lysobisphosphatidic acid (LBPA) which is abundant in MVBs internal membranes. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and enveloped virus budding (HIV-1 and other lentiviruses). Appears to be an adapter for a subset of ESCRT-III proteins, such as CHMP4, to function at distinct membranes. Required for completion of cytokinesis. Involved in HIV-1 virus budding. Can replace TSG101 it its role of supporting HIV-1 release; this function implies the interaction with CHMP4B. May play a role in the regulation of both apoptosis and cell proliferation.<ref>PMID:14505569</ref> <ref>PMID:14505570</ref> <ref>PMID:14739459</ref> <ref>PMID:17853893</ref> <ref>PMID:17428861</ref> <ref>PMID:17556548</ref> [[http://www.uniprot.org/uniprot/CHM4C_HUMAN CHM4C_HUMAN]] Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Involved in HIV-1 p6- and p9-dependent virus release.<ref>PMID:14505569</ref> <ref>PMID:14505570</ref> <ref>PMID:14519844</ref> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Alam, S L]] | ||
+ | [[Category: Sundquist, W I]] | ||
+ | [[Category: Wenzel, D M]] | ||
+ | [[Category: Abscission checkpoint]] | ||
+ | [[Category: Cell division]] | ||
+ | [[Category: Transport protein]] |
Revision as of 07:28, 12 September 2018
CHMP4C in complex with ALIX BRO1
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