1zac
From Proteopedia
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Revision as of 14:28, 30 October 2007
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N-DOMAIN OF TROPONIN C FROM CHICKEN SKELETAL MUSCLE, NMR, MINIMIZED AVERAGE STRUCTURE
Overview
Contractile activity of skeletal muscle is triggered by a Ca2+-induced, "opening" of the regulatory N-domain of troponin C (apo-NTnC residues, 1-90). This structural transition has become a paradigm for large-scale, conformational changes that affect the interaction between proteins. The, regulatory domain is comprised of two basic structural elements: one, contributed by the N-, A-, and D-helices (NAD unit) and the other by the, B- and C-helices (BC unit). The Ca2+-induced opening is characterized by a, movement of the BC unit away from the NAD unit with a concomitant change, in conformation at two hinges (Glu41 and Val65) of the BC unit. To examine, the effect of low temperatures on this Ca2+-induced structural change and, the implications for contractile regulation, we have examined ... [(full description)]
About this Structure
1ZAC is a [Single protein] structure of sequence from [Gallus gallus]. Structure known Active Sites: I and II. Full crystallographic information is available from [OCA].
Reference
Low-temperature-induced structural changes in the Apo regulatory domain of skeletal muscle troponin C., Tsuda S, Miura A, Gagne SM, Spyracopoulos L, Sykes BD, Biochemistry. 1999 May 4;38(18):5693-700. PMID:10231519
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