Crystal structure of the Src family tyrosine kinase Hck

  • Sicheri F
  • Moarefi I
  • Kuriyan J
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Abstract

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.

Author-supplied keywords

  • Amino Acid Sequence Animal Catalysis Cell Line Cry
  • Amino Acid src Homology Domains
  • Molecular Molecular Sequence Data *Protein Confor
  • X-Ray Enzyme Activation Human Models

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Authors

  • F Sicheri

  • I Moarefi

  • J Kuriyan

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