Identifying three-dimensional structures of autophosphorylation complexes in crystals of protein kinases.

ABSTRACT: Protein kinase autophosphorylation is a common regulatory mechanism in cell signaling pathways. Crystal structures of several homomeric protein kinase complexes have a serine, threonine, or tyrosine autophosphorylation site of one kinase monomer located in the active site of another monomer, a structural complex that we call an "autophosphorylation complex." We developed and applied a structural bioinformatics method to identify all such autophosphorylation complexes in x-ray crystallographic structures in the Protein Data Bank (PDB). We identified 15 autophosphorylation complexes in the PDB, of which five complexes had not previously been described in the publications describing the crystal structures. These five complexes consist of tyrosine residues in the N-terminal juxtamembrane regio

SUBMITTER: Xu Q 

PROVIDER: S-EPMC4766099 | biostudies-literature | 2015 Dec

REPOSITORIES: biostudies-literature