Ontology highlight
ABSTRACT:
SUBMITTER: Masterson LR
PROVIDER: S-EPMC2206566 | biostudies-literature | 2008 Jan
REPOSITORIES: biostudies-literature
Proceedings of the National Academy of Sciences of the United States of America 20080104 2
Allosteric signaling in proteins requires long-range communication mediated by highly conserved residues, often triggered by ligand binding. In this article, we map the allosteric network in the catalytic subunit of protein kinase A using NMR spectroscopy. We show that positive allosteric cooperativity is generated by nucleotide and substrate binding during the transitions through the major conformational states: apo, intermediate, and closed. The allosteric network is disrupted by a single site ...[more]