3ggz

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<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=3ggz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ggz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ggz RCSB], [http://www.ebi.ac.uk/pdbsum/3ggz PDBsum]</span></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=3ggz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ggz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ggz RCSB], [http://www.ebi.ac.uk/pdbsum/3ggz PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/IST1_YEAST IST1_YEAST]] Involved in a late step in sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. The lumenal sequestrated membrane proteins are targeted into the vacuole after fusion of the endosome with the vacuole. Regulates the recruitment of VPS4 to the ESCRT-III complex, probably in conjunction with DID2, and VPS4 catalyzes the disassembly of the ESCRT-III complex.<ref>PMID:18032582</ref> <ref>PMID:18032584</ref> [[http://www.uniprot.org/uniprot/DID2_YEAST DID2_YEAST]] Class E VPS protein implicated in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. The lumenal sequestrated membrane proteins will be targeted into the vacuole after fusion of the endosome with the vacuole. Probably acts as a peripherally associated component of the ESCRT-III complex, which appears to be critical for late steps in MVB sorting, such as membrane invagination and final cargo sorting and recruits late-acting components of the sorting machinery. The MVB pathway requires the sequential function of ESCRT-O, -I,-II and -III complex assemblies. Regulates the membrane association of VPS4. Can stimulate VPS4 ATPase activity directly or via VTA1.<ref>PMID:11029042</ref> <ref>PMID:11559748</ref> <ref>PMID:15086794</ref> <ref>PMID:16601096</ref> <ref>PMID:17130288</ref> <ref>PMID:18032584</ref> <ref>PMID:18194652</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 21:24, 24 December 2014

Crystal Structure of S.cerevisiae Ist1 N-terminal domain in complex with Did2 MIM motif

3ggz, resolution 3.80Å

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