Activation segment exchange: a common mechanism of kinase autophosphorylation?
|Abstract||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 ... [truncated at 450 characters in length]|
|Author||Oliver, Antony W; Knapp, Stefan; Pearl, Laurence H;|
|Subject||Animals Crystallography, X-Ray Dimerization Humans Models, Biological Models, Chemical Molecular Conformation Phosphorylation Protein Conformation Protein Structure, Tertiary Protein-Serine-Threonine Kinases Serine Threonine methods chemistry metabolism physiology chemistry chemistry|