Crystal structure of the Src family tyrosine kinase Hck

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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