1ap4
From Proteopedia
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[[Category: troponin c]] | [[Category: troponin c]] | ||
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Revision as of 12:45, 30 October 2007
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REGULATORY DOMAIN OF HUMAN CARDIAC TROPONIN C IN THE CALCIUM-SATURATED STATE, NMR, 40 STRUCTURES
Overview
While calcium binding to troponin C (TnC) triggers the contraction of both, skeletal and cardiac muscle, there is clear evidence that different, mechanisms may be involved. For example, activation of heart myofilaments, occurs with binding to a single regulatory site on TnC, whereas activation, of fast skeletal myofilaments occurs with binding to two regulatory sites., The physiological difference between activation of cardiac and skeletal, myofilaments is not understood at the molecular level due to a lack of, structural details for the response of cardiac TnC to calcium. We, determined the solution structures of the apo and calcium-saturated, regulatory domain of human cardiac TnC by using multinuclear, multidimensional nuclear magnetic resonance spectroscopy. The structure of, apo ... [(full description)]
About this Structure
1AP4 is a [Single protein] structure of sequence from [Homo sapiens] with CA as [ligand]. Structure known Active Site: CUM. Full crystallographic information is available from [OCA].
Reference
Calcium-induced structural transition in the regulatory domain of human cardiac troponin C., Spyracopoulos L, Li MX, Sia SK, Gagne SM, Chandra M, Solaro RJ, Sykes BD, Biochemistry. 1997 Oct 7;36(40):12138-46. PMID:9315850
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