A model structure of the muscle protein complex 4Ca2+.troponin C.troponin I derived from small-angle scattering data: implications for regulation

Biochemistry. 1994 Nov 1;33(43):12800-6. doi: 10.1021/bi00209a011.

Abstract

We report here a model structure for 4Ca2+.troponin C.troponin I derived from small-angle X-ray and neutron scattering data using a Monte Carlo modeling method. In this model, troponin I appears as a spiral structure that wraps around 4Ca2+.troponin C which adopts an extended dumbbell conformation similar to that observed in the crystal structures of troponin C. The troponin I spiral has the approximate dimensions of an alpha-helix and winds through the hydrophobic "cups" in each globular domain of troponin C. The model is consistent with a body of previously published biochemical data on the interactions between troponin C and troponin I, and suggests the molecular mechanism for the Ca(2+)-sensitive switch that regulates the muscle contraction/relaxation cycle involves a signal transmitted via the central spiral region of troponin I.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Calcium / metabolism*
  • Models, Molecular*
  • Molecular Sequence Data
  • Monte Carlo Method
  • Neutrons
  • Protein Conformation
  • Protein Structure, Secondary
  • Scattering, Radiation
  • Troponin / chemistry*
  • Troponin / metabolism*
  • Troponin C
  • Troponin I
  • X-Rays

Substances

  • Troponin
  • Troponin C
  • Troponin I
  • Calcium