• Biology, Medicine
• Published in Molecular cell 2014
• DOI:10.1016/j.molcel.2013.11.013

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

@inproceedings{Chen2014IdentificationOA,
  title={Identification of a Major Determinant for Serine-Threonine Kinase Phosphoacceptor Specificity},
  author={Catherine Chen and Byung Hak Ha and Anastasia F. Th{\'e}venin and Hua Jane Lou and Rong Zhang and Kevin Y. Yip and Jeffrey R Peterson and Mark B Gerstein and Philip M. Kim and Panagis Filippakopoulos and Stefan Knapp and Titus J Boggon and Benjamin E. Turk},
  booktitle={Molecular cell},
  year={2014}
}

• Catherine Chen, Byung Hak Ha, +10 authors Benjamin E. Turk

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 this… CONTINUE READING

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