Entropic contributions and the influence of the hydrophobic environment in promiscuous protein-protein association.

ABSTRACT: The mechanisms by which a promiscuous protein can strongly interact with several different proteins using the same binding interface are not completely understood. An example is protein kinase A (PKA), which uses a single face on its docking/dimerization domain to interact with multiple A-kinase anchoring proteins (AKAP) that localize it to different parts of the cell. In the current study, the configurational entropy contributions to the binding between the AKAP protein HT31 with the D/D domain of RII alpha-regulatory subunit of PKA were examined. The results show that the majority of configurational entropy loss for the interaction was due to decreased fluctuations within rotamer states of the side chains. The result is in contrast to the widely held approximation that the decrease in th

SUBMITTER: Chang CE 

PROVIDER: S-EPMC2391134 | biostudies-literature | 2008 May

REPOSITORIES: biostudies-literature