Superhelical architecture of the myosin filament-linking protein myomesin with unusual elastic properties.

ABSTRACT: Active muscles generate substantial mechanical forces by the contraction/relaxation cycle, and, to maintain an ordered state, they require molecular structures of extraordinary stability. These forces are sensed and buffered by unusually long and elastic filament proteins with highly repetitive domain arrays. Members of the myomesin protein family function as molecular bridges that connect major filament systems in the central M-band of muscle sarcomeres, which is a central locus of passive stress sensing. To unravel the mechanism of molecular elasticity in such filament-connecting proteins, we have determined the overall architecture of the complete C-terminal immunoglobulin domain array of myomesin by X-ray crystallography, electron microscopy, solution X-ray scattering, and atomic force

SUBMITTER: Pinotsis N 

PROVIDER: S-EPMC3279516 | biostudies-literature | 2012 Feb

REPOSITORIES: biostudies-literature