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    J Mol Biol. 1997 Oct 17;273(1):238-55.

    Structural details of a calcium-induced molecular switch: X-ray crystallographic analysis of the calcium-saturated N-terminal domain of troponin C at 1.75 A resolution.

    Strynadka NC, Cherney M, Sielecki AR, Li MX, Smillie LB, James MN.

    Department of Biochemistry, University of Alberta, Edmonton, Canada.

    We have solved and refined the crystal and molecular structures of the calcium-saturated N-terminal domain of troponin C (TnC) to 1.75 A resolution. This has allowed for the first detailed analysis of the calcium binding sites of this molecular switch in the calcium-loaded state. The results provide support for the proposed binding order and qualitatively, for the affinity of calcium in the two regulatory calcium binding sites. Based on a comparison with the high-resolution apo-form of TnC we propose a possible mechanism for the calcium-mediated exposure of a large hydrophobic surface that is central to the initiation of muscle contraction within the cell.

    PMID: 9367759 [PubMed - indexed for MEDLINE]

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