The structural dynamics of α-tropomyosin on F-actin shape the overlap complex between adjacent tropomyosin molecules.

ABSTRACT: Coiled-coil tropomyosin, localized on actin filaments in virtually all eukaryotic cells, serves as a gatekeeper regulating access of the motor protein myosin and other actin-binding proteins onto the thin filament surface. Tropomyosin's modular pseudo-repeating pattern of approximately 39 amino acid residues is designed to allow binding of the coiled-coil to successive actin subunits along thin filaments. Even though different tropomyosin isoforms contain varying numbers of repeat modules, the pseudo-repeat length, in all cases, matches that of a single actin subunit. Thus, the seven pseudo-repeats of 42nm long muscle tropomyosin bind to seven successive actin subunits along thin filaments, while simultaneously bending into a super-helical conformation that is preshaped to the actin filame

SUBMITTER: Lehman W 

PROVIDER: S-EPMC3962804 | biostudies-literature | 2014 Jun

REPOSITORIES: biostudies-literature