The missing links within troponin

Arch Biochem Biophys. 2019 Mar 15:663:95-100. doi: 10.1016/j.abb.2018.12.026. Epub 2018 Dec 22.

Abstract

The cardiac contraction-relaxation cycle is controlled by a sophisticated set of machinery. Of particular interest, is the revelation that allosteric networks transmit effects of binding at one site to influence troponin complex dynamics and structural-mediated signaling in often distal, functional sites in the myofilament. Our recent observations provide compelling evidence that allostery can explain the function of large-scale macromolecular events. Here we elaborate on our recent findings of interdomain communication within troponin C, using cutting-edge structural biology approaches, and highlight the importance of unveiling the unknown, distant communication networks within this system to obtain more comprehensive knowledge of how allostery impacts cardiac physiology and disease.

Keywords: Allostery; Dynamics; Structural biology; Thin filament; Troponin.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Allosteric Regulation
  • Amino Acid Sequence
  • Animals
  • Humans
  • Protein Binding
  • Structure-Activity Relationship
  • Troponin C / chemistry
  • Troponin C / metabolism*
  • Troponin I / chemistry
  • Troponin I / metabolism*

Substances

  • Troponin C
  • Troponin I