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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6617
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pubmed:dateCreated |
1997-3-3
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pubmed:databankReference |
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pubmed:abstractText |
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.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0028-0836
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pubmed:author |
|
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pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
385
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
602-9
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:9024658-Amino Acid Sequence,
pubmed-meshheading:9024658-Animals,
pubmed-meshheading:9024658-Catalysis,
pubmed-meshheading:9024658-Cell Line,
pubmed-meshheading:9024658-Crystallography, X-Ray,
pubmed-meshheading:9024658-Enzyme Activation,
pubmed-meshheading:9024658-Humans,
pubmed-meshheading:9024658-Models, Molecular,
pubmed-meshheading:9024658-Molecular Sequence Data,
pubmed-meshheading:9024658-Protein Conformation,
pubmed-meshheading:9024658-Protein-Tyrosine Kinases,
pubmed-meshheading:9024658-Proto-Oncogene Proteins,
pubmed-meshheading:9024658-Proto-Oncogene Proteins c-hck,
pubmed-meshheading:9024658-Recombinant Proteins,
pubmed-meshheading:9024658-Sequence Homology, Amino Acid,
pubmed-meshheading:9024658-src Homology Domains
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pubmed:year |
1997
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pubmed:articleTitle |
Crystal structure of the Src family tyrosine kinase Hck.
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pubmed:affiliation |
Laboratories of Molecular Biophysics, The Rockefeller University, New York 10021, USA.
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pubmed:publicationType |
Journal Article
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