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} }
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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References
SHOWING 1-10 OF 41 REFERENCES
How do protein kinases discriminate between serine/threonine and tyrosine? Structural insights from the insulin receptor protein‐tyrosine kinase
- Chemistry, Medicine
- FASEB journal : official publication of the Federation of American Societies for Experimental Biology
- 1995
- 170
- PDF
The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases
- Biology, Medicine
- Nature Cell Biology
- 1999
- 493
- PDF
Deciphering Protein Kinase Specificity Through Large-Scale Analysis of Yeast Phosphorylation Site Motifs
- Biology, Medicine
- Science Signaling
- 2010
- 320
- PDF
Tyrosine Versus Serine/Threonine Phosphorylation by Protein Kinase Casein Kinase-2
- Biology, Medicine
- The Journal of Biological Chemistry
- 1999
- 63
- PDF
The influence of basic residues on the substrate specificity of protein kinase C.
- Medicine, Chemistry
- The Journal of biological chemistry
- 1987
- 203
Role of multiple basic residues in determining the substrate specificity of cyclic AMP-dependent protein kinase.
- Chemistry, Medicine
- The Journal of biological chemistry
- 1977
- 591
- PDF
Structural basis and prediction of substrate specificity in protein serine/threonine kinases
- Biology, Medicine
- Proceedings of the National Academy of Sciences of the United States of America
- 2002
- 178
- PDF
Specificity Profiling of Pak Kinases Allows Identification of Novel Phosphorylation Sites*
- Biology, Medicine
- Journal of Biological Chemistry
- 2007
- 122
- PDF
Protein kinase CK2 catalyzes tyrosine phosphorylation in mammalian cells.
- Biology, Medicine
- Cellular signalling
- 2008
- 46
Linear Motif Atlas for Phosphorylation-Dependent Signaling
- Biology, Medicine
- Science Signaling
- 2008
- 396
- PDF