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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 suggest that this phenomenon represents a common mechanism of activation amongst a particular subset of protein kinases, that is, those that are dimeric (either transiently or constitutively), that undergo activation by autophosphorylation and that have activation segment amino acid sequences that do not resemble those of their substrate consensus sequence.

Original publication

DOI

10.1016/j.tibs.2007.06.004

Type

Journal article

Journal

Trends Biochem Sci

Publication Date

08/2007

Volume

32

Pages

351 - 356

Keywords

Animals, Checkpoint Kinase 2, Crystallography, X-Ray, Dimerization, Humans, Models, Biological, Models, Chemical, Molecular Conformation, Phosphorylation, Protein Conformation, Protein Structure, Tertiary, Protein-Serine-Threonine Kinases, Serine, Threonine