4j5l

Structure of the Cargo Binding Domain from Human Myosin Va

spinqualitylabelsall models 4j5l, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4j5l is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4 Related: 4j5m Gene: MYH12, MYO5A (HUMAN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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