Crystal structure of the Src family tyrosine kinase Hck

F Sicheri; I Moarefi; J Kuriyan

doi:10.1038/385602a0

Crystal structure of the Src family tyrosine kinase Hck

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

Authors

F Sicheri¹, I Moarefi, J Kuriyan

Affiliation

¹ Laboratories of Molecular Biophysics, The Rockefeller University, New York 10021, USA.

PMID: 9024658
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 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

Substances

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

Associated data

PDB/UNKNOWN