5j8e
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5j8e]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J8E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J8E FirstGlance]. <br> | <table><tr><td colspan='2'>[[5j8e]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J8E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J8E 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=5j8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j8e OCA], [http://pdbe.org/5j8e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j8e RCSB], [http://www.ebi.ac.uk/pdbsum/5j8e PDBsum]</span></td></tr> | + | </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=5j8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j8e OCA], [http://pdbe.org/5j8e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j8e RCSB], [http://www.ebi.ac.uk/pdbsum/5j8e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j8e ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/HOOK3_HUMAN HOOK3_HUMAN]] Probably serves as a target for the spiC protein from Salmonella typhimurium, which inactivates it, leading to a strong alteration in cellular trafficking (By similarity). Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). May regulate clearance of endocytosed receptors such as MSR1. Participates in defining the architecture and localization of the Golgi complex.<ref>PMID:11238449</ref> <ref>PMID:17237231</ref> <ref>PMID:18799622</ref> | [[http://www.uniprot.org/uniprot/HOOK3_HUMAN HOOK3_HUMAN]] Probably serves as a target for the spiC protein from Salmonella typhimurium, which inactivates it, leading to a strong alteration in cellular trafficking (By similarity). Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). May regulate clearance of endocytosed receptors such as MSR1. Participates in defining the architecture and localization of the Golgi complex.<ref>PMID:11238449</ref> <ref>PMID:17237231</ref> <ref>PMID:18799622</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Metazoan cytoplasmic dynein moves processively along microtubules with the aid of dynactin and an adaptor protein that joins dynein and dynactin into a stable ternary complex. Here, we examined how Hook3, a cargo adaptor involved in Golgi and endosome transport, forms a motile dynein-dynactin complex. We show that the conserved Hook domain interacts directly with the dynein light intermediate chain 1 (LIC1). By solving the crystal structure of the Hook domain and using structure-based mutagenesis, we identify two conserved surface residues that are each critical for LIC1 binding. Hook proteins with mutations in these residues fail to form a stable dynein-dynactin complex, revealing a crucial role for LIC1 in this interaction. We also identify a region of Hook3 specifically required for an allosteric activation of processive motility. Our work reveals the structural details of Hook3's interaction with dynein and offers insight into how cargo adaptors form processive dynein-dynactin motor complexes. | ||
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| + | Assembly and activation of dynein-dynactin by the cargo adaptor protein Hook3.,Schroeder CM, Vale RD J Cell Biol. 2016 Aug 1;214(3):309-18. doi: 10.1083/jcb.201604002. PMID:27482052<ref>PMID:27482052</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5j8e" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 05:23, 9 September 2016
Crystal structure of human Hook3's conserved Hook domain
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