1TNP

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

Summary for 1TNP

• Entry DOI: 10.2210/pdb1tnp/pdb
• Descriptor: TROPONIN-C (APO) (1 entity in total)
• Functional Keywords: ef-hand, calcium-binding protein
• Biological source: Gallus gallus (chicken)
• Total number of polymer chains: 1
• Total formula weight: 9984.08

Authors

Gagne, S.M.,Sykes, B.D. (deposition date: 1995-07-07, release date: 1995-10-15, Last modification date: 2024-05-22)

Primary citation

Gagne, S.M.,Tsuda, S.,Li, M.X.,Smillie, L.B.,Sykes, B.D.
Structures of the troponin C regulatory domains in the apo and calcium-saturated states.
Nat.Struct.Biol., 2:784-789, 1995

PubMed Abstract: 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.

PubMed: 7552750
DOI: 10.1038/nsb0995-784

Experimental method

SOLUTION NMR