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