2g9j

Complex of TM1a(1-14)Zip with TM9a(251-284): a model for the polymerization domain ("overlap region") of tropomyosin, Northeast Structural Genomics Target OR9

spinqualitylabelsall models 2g9j, 10 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2g9j is a 4 chain structure with sequence from Rattus norvegicus and Saccharomyces cerevisiae. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1tmz, 1mv4 Gene: TPM1 (Rattus norvegicus), TPM1 (Saccharomyces cerevisiae) Resources: FirstGlance, OCA, RCSB, PDBsum, TOPSAN Function [TPM1_RAT] Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Tropomyosin is a coiled-coil protein that binds head-to-tail along the length of actin filaments in eukaryotic cells, stabilizing them and providing protection from severing proteins. Tropomyosin cooperatively regulates actin's interaction with myosin and mediates the Ca2+ -dependent regulation of contraction by troponin in striated muscles. The N-terminal and C-terminal ends are critical functional determinants that form an "overlap complex". Here we report the solution NMR structure of an overlap complex formed of model peptides. In the complex, the chains of the C-terminal coiled coil spread apart to allow insertion of 11 residues of the N-terminal coiled coil into the resulting cleft. The plane of the N-terminal coiled coil is rotated 90 degrees relative to the plane of the C terminus. A consequence of the geometry is that the orientation of postulated periodic actin binding sites on the coiled-coil surface is retained from one molecule to the next along the actin filament when the overlap complex is modeled into the X-ray structure of tropomyosin determined at 7 Angstroms. Nuclear relaxation NMR data reveal flexibility of the junction, which may function to optimize binding along the helical actin filament and to allow mobility of tropomyosin on the filament surface as it switches between regulatory states. Solution NMR structure of the junction between tropomyosin molecules: implications for actin binding and regulation.,Greenfield NJ, Huang YJ, Swapna GV, Bhattacharya A, Rapp B, Singh A, Montelione GT, Hitchcock-DeGregori SE J Mol Biol. 2006 Nov 17;364(1):80-96. Epub 2006 Aug 17. PMID:16999976 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Gcn4 Tropomyosin

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