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==Overview==
==Overview==
The crystal structure of the haematopoietic cell kinase Hck has been, determined at 2.6/2.9 A 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.
The crystal structure of the haematopoietic cell kinase Hck has been determined at 2.6/2.9 A 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.


==About this Structure==
==About this Structure==
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[[Category: tyrosine-protein kinase]]
[[Category: tyrosine-protein kinase]]


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