Document Detail

Crystal structure of the Src family tyrosine kinase Hck.
MedLine Citation:
PMID:  9024658     Owner:  NLM     Status:  MEDLINE    
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.
F Sicheri; I Moarefi; J Kuriyan
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Nature     Volume:  385     ISSN:  0028-0836     ISO Abbreviation:  Nature     Publication Date:  1997 Feb 
Date Detail:
Created Date:  1997-03-03     Completed Date:  1997-03-03     Revised Date:  2012-06-05    
Medline Journal Info:
Nlm Unique ID:  0410462     Medline TA:  Nature     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  602-9     Citation Subset:  IM    
Laboratories of Molecular Biophysics, The Rockefeller University, New York 10021, USA.
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MeSH Terms
Amino Acid Sequence
Cell Line
Crystallography, X-Ray
Enzyme Activation
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
Reg. No./Substance:
0/Proto-Oncogene Proteins; 0/Recombinant Proteins; EC Kinases; EC protein, human; EC Proteins c-hck
Comment In:
Nature. 1997 Feb 13;385(6617):582-3, 585   [PMID:  9024653 ]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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