6e5n

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<StructureSection load='6e5n' size='340' side='right'caption='[[6e5n]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='6e5n' size='340' side='right'caption='[[6e5n]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6e5n]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E5N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E5N FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6e5n]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E5N OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6E5N FirstGlance]. <br>
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</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=6e5n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e5n OCA], [http://pdbe.org/6e5n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e5n RCSB], [http://www.ebi.ac.uk/pdbsum/6e5n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e5n ProSAT]</span></td></tr>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MYO6, KIAA0389 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CLTA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6e5n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e5n OCA], [http://pdbe.org/6e5n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e5n RCSB], [http://www.ebi.ac.uk/pdbsum/6e5n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e5n ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/MYO6_HUMAN MYO6_HUMAN]] Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Myosin 6 is a reverse-direction motor protein that moves towards the minus-end of actin filaments. Has slow rate of actin-activated ADP release due to weak ATP binding. Functions in a variety of intracellular processes such as vesicular membrane trafficking and cell migration. Required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. May act as a regulator of F-actin dynamics. May play a role in transporting DAB2 from the plasma membrane to specific cellular targets. Required for structural integrity of inner ear hair cells (By similarity).<ref>PMID:10519557</ref> <ref>PMID:11447109</ref> <ref>PMID:16507995</ref> <ref>PMID:16949370</ref> [[http://www.uniprot.org/uniprot/CLCA_HUMAN CLCA_HUMAN]] Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Acts as component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge (PubMed:15858577, PubMed:21297582).<ref>PMID:15858577</ref> <ref>PMID:21297582</ref>
[[http://www.uniprot.org/uniprot/MYO6_HUMAN MYO6_HUMAN]] Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Myosin 6 is a reverse-direction motor protein that moves towards the minus-end of actin filaments. Has slow rate of actin-activated ADP release due to weak ATP binding. Functions in a variety of intracellular processes such as vesicular membrane trafficking and cell migration. Required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. May act as a regulator of F-actin dynamics. May play a role in transporting DAB2 from the plasma membrane to specific cellular targets. Required for structural integrity of inner ear hair cells (By similarity).<ref>PMID:10519557</ref> <ref>PMID:11447109</ref> <ref>PMID:16507995</ref> <ref>PMID:16949370</ref> [[http://www.uniprot.org/uniprot/CLCA_HUMAN CLCA_HUMAN]] Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Acts as component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge (PubMed:15858577, PubMed:21297582).<ref>PMID:15858577</ref> <ref>PMID:21297582</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Clathrin light chains (CLCa and CLCb) are major constituents of clathrin-coated vesicles. Unique functions for these evolutionary conserved paralogs remain elusive, and their role in clathrin-mediated endocytosis in mammalian cells is debated. Here, we find and structurally characterize a direct and selective interaction between CLCa and the long isoform of the actin motor protein myosin VI, which is expressed exclusively in highly polarized tissues. Using genetically-reconstituted Caco-2 cysts as proxy for polarized epithelia, we provide evidence for coordinated action of myosin VI and CLCa at the apical surface where these proteins are essential for fission of clathrin-coated pits. We further find that myosin VI and Huntingtin-interacting protein 1-related protein (Hip1R) are mutually exclusive interactors with CLCa, and suggest a model for the sequential function of myosin VI and Hip1R in actin-mediated clathrin-coated vesicle budding.
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Clathrin light chain A drives selective myosin VI recruitment to clathrin-coated pits under membrane tension.,Biancospino M, Buel GR, Nino CA, Maspero E, Scotto di Perrotolo R, Raimondi A, Redlingshofer L, Weber J, Brodsky FM, Walters KJ, Polo S Nat Commun. 2019 Oct 31;10(1):4974. doi: 10.1038/s41467-019-12855-6. PMID:31672988<ref>PMID:31672988</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6e5n" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Buel, G R]]
[[Category: Buel, G R]]

Revision as of 06:31, 3 June 2020

Solution structure of human Myosin VI isoform 3 (1050-1131) in complex with Clathrin light chain a (46-61)

PDB ID 6e5n

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