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Crystal structure of the Src family tyrosine kinase Hck

Nature volume 385, pages 602–609 (1997)Cite this article

Abstract

The crystal structure of the haematopoietic cell kinase Hck has been determined at 2.6/2.9 Å resolution. Inhibition of enzymatic activity is a consequence of intramolecular interactions of the enzyme's Src-homology domains SH2 and SH3, with concomitant displacement of elements of the catalytic domain. The conformation of the active site has similarities with that of inactive cyclin-dependent protein kinases.

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Author information

Author notes

  1. Frank Sicheri and Ismail Moarefi: These authors contributed equally to this work.

Authors and Affiliations

  1. Laboratories of Molecular Biophysics, The Rockefeller University, 1230 York Avenue, New York, New York, 10021, USA

    Ismail Moarefi & John Kuriyan

  2. Howard Hughes Medical Institute, The Rockefeller University, 1230 York Avenue, New York, New York, 10021, USA

    Ismail Moarefi & John Kuriyan

Authors
  1. Frank Sicheri
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  2. Ismail Moarefi
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  3. John Kuriyan
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Sicheri, F., Moarefi, I. & Kuriyan, J. Crystal structure of the Src family tyrosine kinase Hck. Nature 385, 602–609 (1997). https://doi.org/10.1038/385602a0

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