4j5l: Difference between revisions
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==Structure of the Cargo Binding Domain from Human Myosin Va== | |||
<StructureSection load='4j5l' size='340' side='right' caption='[[4j5l]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4j5l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J5L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4J5L FirstGlance]. <br> | |||
==Disease== | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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='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> | |||
</table> | |||
== Disease == | |||
[[http://www.uniprot.org/uniprot/MYO5A_HUMAN 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. | [[http://www.uniprot.org/uniprot/MYO5A_HUMAN 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 == | |||
[[http://www.uniprot.org/uniprot/MYO5A_HUMAN 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.<ref>PMID:10448864</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Myosin 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<ref>PMID:24097982</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== | ==See Also== | ||
*[[Myosin|Myosin]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Assis, L H.P | [[Category: Assis, L H.P]] | ||
[[Category: Berridge, G | [[Category: Berridge, G]] | ||
[[Category: Burgess-Brown, N | [[Category: Burgess-Brown, N]] | ||
[[Category: Delft, F von | [[Category: Delft, F von]] | ||
[[Category: Krojer, T | [[Category: Krojer, T]] | ||
[[Category: Mahajan, P | [[Category: Mahajan, P]] | ||
[[Category: Murakami, M T | [[Category: Murakami, M T]] | ||
[[Category: Nascimento, A F.Z | [[Category: Nascimento, A F.Z]] | ||
[[Category: Tonoli, C C.C | [[Category: Tonoli, C C.C]] | ||
[[Category: Trindade, D M | [[Category: Trindade, D M]] | ||
[[Category: Vollmar, M | [[Category: Vollmar, M]] | ||
[[Category: C-terminal globular tail]] | [[Category: C-terminal globular tail]] | ||
[[Category: Human myosin va]] | [[Category: Human myosin va]] | ||
Revision as of 20:19, 21 December 2014
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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