4j5l: Difference between revisions
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==Structure of the Cargo Binding Domain from Human Myosin Va== | ==Structure of the Cargo Binding Domain from Human Myosin Va== | ||
<StructureSection load='4j5l' size='340' side='right' caption='[[4j5l]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='4j5l' size='340' side='right' caption='[[4j5l]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4j5m|4j5m]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4j5m|4j5m]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MYH12, MYO5A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MYH12, MYO5A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4j5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j5l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4j5l RCSB], [http://www.ebi.ac.uk/pdbsum/4j5l 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=4j5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j5l OCA], [http://pdbe.org/4j5l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4j5l RCSB], [http://www.ebi.ac.uk/pdbsum/4j5l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4j5l ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4j5l" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 09:11, 5 August 2016
Structure of the Cargo Binding Domain from Human Myosin VaStructure of the Cargo Binding Domain from Human Myosin Va
Structural highlights
Disease[MYO5A_HUMAN] Griscelli disease type 3;Neuroectodermal melanolysosomal disease;Griscelli disease type 1. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. Function[MYO5A_HUMAN] Processive actin-based motor that can move in large steps approximating the 36-nm pseudo-repeat of the actin filament. Involved in melanosome transport. Also mediates the transport of vesicles to the plasma membrane. May also be required for some polarization process involved in dendrite formation.[1] Publication Abstract from PubMedMyosin V (MyoV) motors have been implicated in the intracellular transport of diverse cargoes including vesicles, organelles, RNA-protein complexes and regulatory proteins. Here, we have solved the cargo-binding domain (CBD) structures of the three human MyoV paralogs (Va, Vb and Vc), revealing subtle structural changes that drive functional differentiation and a novel redox mechanism controlling the CBD dimerization process, which is unique for the MyoVc subclass. Moreover, the cargo- and motor-binding sites were structurally assigned indicating the conservation of residues involved in the recognition of adaptors for peroxisome transport and providing high-resolution insights into motor domain (MD) inhibition by CBD. These results contribute to understanding the structural requirements for cargo transport, auto-inhibition and regulatory mechanisms in myosin V motors. Structural insights into functional overlapping and differentiation among myosin V motors.,Nascimento AF, Trindade DM, Tonoli CC, de Giuseppe PO, Assis LH, Honorato RV, de Oliveira PS, Mahajan P, Burgess-Brown NA, von Delft F, Larson RE, Murakami MT J Biol Chem. 2013 Oct 4. PMID:24097982[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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