Structural basis of regulation and substrate specificity of protein kinase CK2 deduced from the modeling of protein-protein interactions.

ABSTRACT:

Background

Protein Kinase Casein Kinase 2 (PKCK2) is an ubiquitous Ser/Thr kinase expressed in all eukaryotes. It phosphorylates a number of proteins involved in various cellular processes. PKCK2 holoenzyme is catalytically active tetramer, composed of two homologous or identical and constitutively active catalytic (alpha) and two identical regulatory (beta) subunits. The tetramer cannot phosphorylate some substrates that can be phosphorylated by PKCK2alpha in isolation. The present work explores the structural basis of this feature using computational analysis and modeling.

Results

We have initially built a model of PKCK2alpha bound to a substrate peptide with a conformation identical to that of the substrates in the available crystal structures of other kinases complexed w

SUBMITTER: Rekha N 

PROVIDER: S-EPMC161795 | biostudies-literature | 2003 May

REPOSITORIES: biostudies-literature