Xin Huang

Harvard Medical School, Boston, Massachusetts, United States

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Publications (1)6.59 Total impact

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    ABSTRACT: The direct substrates of one protein kinase in a cell can be identified by mutation of the ATP binding pocket to allow an unnatural ATP analog to be accepted exclusively by the engineered kinase. Here, we present structural and functional assessment of peptide specificity of mutant protein kinases with unnatural ATP analogs. The crystal structure (2.8 A resolution) of c-Src (T338G) with N(6)-(benzyl) ADP bound shows that the creation of a unique nucleotide binding pocket does not alter the phospho-acceptor binding site of the kinase. A panel of optimal peptide substrates of defined sequence, as well as a degenerate peptide library, was utilized to assess the phospho-acceptor specificity of the engineered "traceable" kinases. The specificity profiles for the mutant kinases were found to be identical to those of their wild-type counterparts.
    Chemistry & Biology 02/2002; 9(1):25-33. DOI:10.1016/S1074-5521(02)00091-1 · 6.59 Impact Factor

Publication Stats

41 Citations
6.59 Total Impact Points

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Institutions

  • 2002
    • Harvard Medical School
      • Department of Biological Chemistry and Molecular Pharmacology
      Boston, Massachusetts, United States