3pzd
Structure of the myosin X MyTH4-FERM/DCC complexStructure of the myosin X MyTH4-FERM/DCC complex
FunctionFunction
[MYO10_HUMAN] Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. MYO10 binds to actin filaments and actin bundles and functions as plus end-directed motor. The tail domain binds to membranous compartments containing phosphatidylinositol 3,4,5-trisphosphate or integrins, and mediates cargo transport along actin filaments. Regulates cell shape, cell spreading and cell adhesion. Stimulates the formation and elongation of filopodia. May play a role in neurite outgrowth and axon guidance. Plays a role in formation of the podosome belt in osteoclasts (By similarity).[1] [DCC_MOUSE] Receptor for netrin required for axon guidance. Mediates axon attraction of neuronal growth cones in the developing nervous system upon ligand binding. Its association with UNC5 proteins may trigger signaling for axon repulsion. It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand. Implicated as a tumor suppressor gene.
About this StructureAbout this Structure
3pzd is a 2 chain structure with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.
See AlsoSee Also
ReferenceReference
- ↑ Wei Z, Yan J, Lu Q, Pan L, Zhang M. Cargo recognition mechanism of myosin X revealed by the structure of its tail MyTH4-FERM tandem in complex with the DCC P3 domain. Proc Natl Acad Sci U S A. 2011 Mar 1;108(9):3572-7. Epub 2011 Feb 14. PMID:21321230 doi:10.1073/pnas.1016567108
- ↑ Bohil AB, Robertson BW, Cheney RE. Myosin-X is a molecular motor that functions in filopodia formation. Proc Natl Acad Sci U S A. 2006 Aug 15;103(33):12411-6. Epub 2006 Aug 7. PMID:16894163 doi:10.1073/pnas.0602443103