| Literature DB >> 27395017 |
Lauren Ann Metskas1, Elizabeth Rhoades2.
Abstract
The troponin complex is a molecular switch that ties shifting intracellular calcium concentration to association and dissociation of actin and myosin, effectively allowing excitation-contraction coupling in striated muscle. Although there is a long history of muscle biophysics and structural biology, many of the mechanistic details that enable troponin's function remain incompletely understood. This review summarizes the current structural understanding of the troponin complex on the muscle thin filament, focusing on conformational changes in flexible regions of the troponin I subunit. In particular, we focus on order-disorder transitions in the C-terminal domain of troponin I, which have important implications in cardiac disease and could also have potential as a model system for the study of coupled binding and folding.Entities:
Keywords: coupled binding and folding; disordered proteins; hypertrophic cardiomyopathy; troponin; troponin I mobile domain
Mesh:
Substances:
Year: 2016 PMID: 27395017 PMCID: PMC4976047 DOI: 10.1016/j.jmb.2016.06.022
Source DB: PubMed Journal: J Mol Biol ISSN: 0022-2836 Impact factor: 5.469