The flexibility of two tropomyosin mutants, D175N and E180G, that cause hypertrophic cardiomyopathy.

ABSTRACT: Point mutations targeting muscle thin filament proteins are the cause of a number of cardiomyopathies. In many cases, biological effects of the mutations are well-documented, whereas their structural and mechanical impact on filament assembly and regulatory function is lacking. In order to elucidate molecular defects leading to cardiac dysfunction, we have examined the structural mechanics of two tropomyosin mutants, E180G and D175N, which are associated with hypertrophic cardiomyopathy (HCM). Tropomyosin is an α-helical coiled-coil dimer which polymerizes end-to-end to create an elongated superhelix that wraps around F-actin filaments of muscle and non-muscle cells, thus modulating the binding of other actin-binding proteins. Here, we study how flexibility changes in the E180G and D175N m

SUBMITTER: Li XE 

PROVIDER: S-EPMC3412897 | biostudies-literature | 2012 Aug

REPOSITORIES: biostudies-literature