Nature 385, 602 - 609 (13 February 1997); doi:10.1038/385602a0

Crystal structure of the Src family tyrosine kinase Hck

Frank Sicheri^†, Ismail Moarefi^*† & John Kuriyan^*

Laboratories of Molecular Biophysics, and ^* Howard Hughes Medical Institute, The Rockefeller University, 1230 York Avenue, New York, New York 10021, USA
^† These authors contributed equally to this work.

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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