Crystal structure of the Src family tyrosine kinase Hck

Nature. 1997 Feb 13;385(6617):602-9. doi: 10.1038/385602a0.


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.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Catalysis
  • Cell Line
  • Crystallography, X-Ray
  • Enzyme Activation
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation*
  • Protein-Tyrosine Kinases / chemistry*
  • Proto-Oncogene Proteins / chemistry*
  • Proto-Oncogene Proteins c-hck
  • Recombinant Proteins / chemistry
  • Sequence Homology, Amino Acid
  • src Homology Domains


  • Proto-Oncogene Proteins
  • Recombinant Proteins
  • Protein-Tyrosine Kinases
  • HCK protein, human
  • Proto-Oncogene Proteins c-hck

Associated data