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Primary citation
Title Crystal structure of the Src family tyrosine kinase Hck.
Authors Sicheri, F.search; Moarefi, I.search; Kuriyan, J.search
Journal NATUREsearch vol:385, pag:602-609 (1997), Identifiers: PubMed ID (9024658)search DOI (10.1038/385602a0)
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 Amino Acid Sequencesearch, Animalssearch, Catalysissearch, Cell Linesearch, Crystallographysearch, X-Raysearch, Enzyme Activationsearch, Humanssearch, Modelssearch, Molecularsearch, Molecular Sequence Datasearch, Protein Conformationsearch, Protein-Tyrosine Kinasessearch, Proto-Oncogene Proteinssearch, Proto-Oncogene Proteins c-hcksearch, Recombinant Proteinssearch, Sequence Homologysearch, Amino Acidsearch, src Homology Domainssearch
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