Ontology highlight
ABSTRACT:
SUBMITTER: Brown JH
PROVIDER: S-EPMC1323185 | biostudies-literature | 2005 Dec
REPOSITORIES: biostudies-literature
Brown Jerry H JH Zhou Zhaocai Z Reshetnikova Ludmilla L Robinson Howard H Yammani Rama D RD Tobacman Larry S LS Cohen Carolyn C
Proceedings of the National Academy of Sciences of the United States of America 20051219 52
Tropomyosin is a two-chain alpha-helical coiled coil whose periodic interactions with the F-actin helix are critical for thin filament stabilization and the regulation of muscle contraction. Here we deduce the mechanical and chemical basis of these interactions from the 2.3-A-resolution crystal structure of the middle three of tropomyosin's seven periods. Geometrically specific bends of the coiled coil, produced by clusters of core alanines, and variable bends about gaps in the core, produced by ...[more]