Ontology highlight
ABSTRACT:
SUBMITTER: Masterson LR
PROVIDER: S-EPMC3487389 | biostudies-literature | 2010 Nov
REPOSITORIES: biostudies-literature
Masterson Larry R LR Cheng Cecilia C Yu Tao T Tonelli Marco M Kornev Alexandr A Taylor Susan S SS Veglia Gianluigi G
Nature chemical biology 20101003 11
Atomic resolution studies of protein kinases have traditionally been carried out in the inhibitory state, limiting our current knowledge on the mechanisms of substrate recognition and catalysis. Using NMR, X-ray crystallography and thermodynamic measurements, we analyzed the substrate recognition process of cAMP-dependent protein kinase (PKA), finding that entropy and protein dynamics play a prominent role. The nucleotide acts as a dynamic and allosteric activator by coupling the two lobes of ap ...[more]