Activation segment exchange: a common mechanism of kinase autophosphorylation?

Journal article

The crystal structure of the kinase domain from human checkpoint kinase 2 (Chk2) has shown, for the first time, the reciprocal exchange of activation segments between two adjacent molecules and provides the molecular basis for understanding the observed mode of Chk2 kinase activation via trans-autophosphorylation. With further examples of activation segment exchanged kinase domains now publicly available (i.e. Ste20-like kinase, Ser/Thr kinase 10 and Death-associated protein kinase 3), we sug...

Expand abstract

Authors: Oliver, A; Knapp, S; Pearl, L

• Publication status: Published
• Journal: Trends in biochemical sciences
• Volume: 32
• Issue: 8
• Pages: 351-356
• Publication date: 2007-08-01
• DOI: 10.1016/j.tibs.2007.06.004
• ISSN: 0968-0004
• Language: English
• Keywords: Models, Chemical; Protein-Serine-Threonine Kinases; Models, Biological; Humans; Crystallography, X-Ray; Protein Structure, Tertiary; Protein Conformation; Animals; Phosphorylation; Threonine; Molecular Conformation; Serine; Dimerization