• DOI:10.1016/j.molcel.2013.11.013
Corpus ID: 7770696

Identification of a Major Determinant for Serine-Threonine Kinase Phosphoacceptor Specificity

@article{Chen2014IdentificationOA,
  title={Identification of a Major Determinant for Serine-Threonine Kinase Phosphoacceptor Specificity},
  author={Catherine Chen and B. Ha and Anastasia F. Th{\'e}venin and H. J. Lou and R. Zhang and K. Yip and J. Peterson and M. Gerstein and P. M. Kim and P. Filippakopoulos and S. Knapp and T. Boggon and B. Turk},
  journal={Molecular Cell},
  year={2014},
  volume={53},
  pages={140 - 147}
}

Catherine Chen, B. Ha, +10 authors B. Turk

Published 2014

Biology, Medicine

Molecular Cell

Summary Eukaryotic protein kinases are generally classified as being either tyrosine or serine-threonine specific. Though not evident from inspection of their primary sequences, many serine-threonine kinases display a significant preference for serine or threonine as the phosphoacceptor residue. Here we show that a residue located in the kinase activation segment, which we term the “DFG+1” residue, acts as a major determinant for serine-threonine phosphorylation site specificity. Mutation of… CONTINUE READING

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