Ontology highlight
ABSTRACT:
SUBMITTER: Biondi RM
PROVIDER: S-EPMC305637 | biostudies-literature | 2000 Mar
REPOSITORIES: biostudies-literature
Biondi R M RM Cheung P C PC Casamayor A A Deak M M Currie R A RA Alessi D R DR
The EMBO journal 20000301 5
The 3-phosphoinositide-dependent protein kinase-1 (PDK1) phosphorylates and activates a number of protein kinases of the AGC subfamily. The kinase domain of PDK1 interacts with a region of protein kinase C-related kinase-2 (PRK2), termed the PDK1-interacting fragment (PIF), through a hydrophobic motif. Here we identify a hydrophobic pocket in the small lobe of the PDK1 kinase domain, separate from the ATP- and substrate-binding sites, that interacts with PIF. Mutation of residues predicted to fo ...[more]