Ontology highlight
ABSTRACT:
SUBMITTER: Dettori R
PROVIDER: S-EPMC2781587 | biostudies-literature | 2009 Oct
REPOSITORIES: biostudies-literature
Dettori Rosalia R Sonzogni Silvina S Meyer Lucas L Lopez-Garcia Laura A LA Morrice Nick A NA Zeuzem Stefan S Engel Matthias M Piiper Albrecht A Neimanis Sonja S Frödin Morten M Biondi Ricardo M RM
The Journal of biological chemistry 20090901 44
The members of the AGC kinase family frequently exhibit three conserved phosphorylation sites: the activation loop, the hydrophobic motif (HM), and the zipper (Z)/turn-motif (TM) phosphorylation site. 3-Phosphoinositide-dependent protein kinase 1 (PDK1) phosphorylates the activation loop of numerous AGC kinases, including the protein kinase C-related protein kinases (PRKs). Here we studied the docking interaction between PDK1 and PRK2 and analyzed the mechanisms that regulate this interaction. I ...[more]