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2n9b
From Proteopedia
Solution NMR Structure of Antiparallel Myosin-10:GCN4 Tandem Coiled-Coil
Structural highlights
Function[MYO10_BOVIN] In hippocampal neurons it induces the formation of dendritic filopodia by trafficking the actin-remodeling protein VASP to the tips of filopodia, where it promotes actin elongation (By similarity). 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, which are then moved relative to actin filaments. Stimulates the formation and elongation of filopodia. Regulates cell shape, cell spreading and cell adhesion. Plays a role in formation of the podosome belt in osteoclasts.[1] [2] [3] [4] [5] [6] [7] [8] [9] Publication Abstract from PubMedCoiled-coil fusions are a useful approach to enforce dimerization in protein engineering. However, the final structures of coiled-coil fusion proteins have received relatively little attention. Here, we determine the structural outcome of adjacent parallel and antiparallel coiled coils. The targets are coiled coils that stabilize myosin-10 in single-molecule biophysical studies. We reveal the solution structure of a short, antiparallel, myosin-10 coiled-coil fused to the parallel GCN4-p1 coiled coil. Surprisingly, this structure is a continuous, antiparallel coiled coil where GCN4-p1 pairs with myosin-10 rather than itself. We also show that longer myosin-10 segments in these parallel/antiparallel fusions are dynamic and do not fold cooperatively. Our data resolve conflicting results on myosin-10 selection of actin filament bundles, demonstrating the importance of understanding coiled-coil orientation and stability. Competition between Coiled-Coil Structures and the Impact on Myosin-10 Bundle Selection.,Vavra KC, Xia Y, Rock RS Biophys J. 2016 Jun 7;110(11):2517-2527. doi: 10.1016/j.bpj.2016.04.048. PMID:27276269[10] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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