4l8t | pdb_00004l8t

Structure of the Cargo Binding Domain from Human Myosin Vc

spinqualitylabelsall models 4l8t, resolution 2.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4l8t is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 4j5l, 4j5m Gene: MYO5C (HUMAN) Resources: FirstGlance, OCA, RCSB, PDBsum Function [MYO5C_HUMAN] May be involved in transferrin trafficking. Likely to power actin-based membrane trafficking in many physiologically crucial tissues. 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. See Also Myosin

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