1tnp | pdb_00001tnp

STRUCTURES OF THE APO AND CALCIUM TROPONIN-C REGULATORY DOMAINS: THE MUSCLE CONTRACTION SWITCH

spinqualitylabelsall models 1tnp, 40 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1tnp is a 1 chain structure with sequence from Chick. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: NTNC (CHICK) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [TNNC2_CHICK] Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on 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 Regulation of contraction in skeletal muscle occurs through calcium binding to the protein troponin C. The solution structures of the regulatory domain of apo and calcium-loaded troponin C have been determined by multinuclear, multidimensional nuclear magnetic resonance techniques. The structural transition in the regulatory domain of troponin C on calcium binding involves an opening of the structure through large changes in interhelical angles. This leads to the increased exposure of an extensive hydrophobic patch, an event that triggers skeletal muscle contraction. Structures of the troponin C regulatory domains in the apo and calcium-saturated states.,Gagne SM, Tsuda S, Li MX, Smillie LB, Sykes BD Nat Struct Biol. 1995 Sep;2(9):784-9. PMID:7552750 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Troponin

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