Crystal structure of the Src family tyrosine kinase Hck
- 1 February 1997
- journal article
- Published by Springer Nature in Nature
- Vol. 385 (6617) , 602-609
- https://doi.org/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.Keywords
This publication has 43 references indexed in Scilit:
- Regulation, substrates and functions of srcBiochimica et Biophysica Acta (BBA) - Reviews on Cancer, 1996
- Deficiency of the Hck and Src tyrosine kinases results in extreme levels of extramedullary hematopoiesisBlood, 1996
- Protein modules and signalling networksNature, 1995
- Modular binding domains in signal transduction proteinsCell, 1995
- Functional overlap in the src gene family: inactivation of hck and fgr impairs natural immunity.Genes & Development, 1994
- Crystal structure of a Src-homology 3 (SH3) domainNature, 1992
- Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptidesNature, 1992
- Crystal Structure of the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein KinaseScience, 1991
- Identification of a human gene (HCK) that encodes a protein-tyrosine kinase and is expressed in hemopoietic cells.Molecular and Cellular Biology, 1987
- Novel protein-tyrosine kinase gene (hck) preferentially expressed in cells of hematopoietic origin.Molecular and Cellular Biology, 1987