Ontology highlight
ABSTRACT:
SUBMITTER: Vigil D
PROVIDER: S-EPMC2242374 | biostudies-literature | 2006 Jan
REPOSITORIES: biostudies-literature
Vigil Dominico D Lin Jung-Hsin JH Sotriffer Christoph A CA Pennypacker Juniper K JK McCammon J Andrew JA Taylor Susan S SS
Protein science : a publication of the Protein Society 20051201 1
Cyclic AMP activates protein kinase A by binding to an inhibitory regulatory (R) subunit and releasing inhibition of the catalytic (C) subunit. Even though crystal structures of regulatory and catalytic subunits have been solved, the precise molecular mechanism by which cyclic AMP activates the kinase remains unknown. The dynamic properties of the cAMP binding domain in the absence of cAMP or C-subunit are also unknown. Here we report molecular-dynamics simulations and mutational studies of the ...[more]