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Crystal structure of the Src family tyrosine kinase Hck

Crystal structure of the Src family tyrosine kinase Hck The crystal structure of the haematopoietic cell kinase Hck has been determined at 2.6/2.9 Å 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Nature Springer Journals

Crystal structure of the Src family tyrosine kinase Hck

Nature , Volume 385 (6617) – Feb 13, 1997

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References (50)

Publisher
Springer Journals
Copyright
Copyright © 1997 by Nature Publishing Group
Subject
Science, Humanities and Social Sciences, multidisciplinary; Science, Humanities and Social Sciences, multidisciplinary; Science, multidisciplinary
ISSN
0028-0836
eISSN
1476-4687
DOI
10.1038/385602a0
Publisher site
See Article on Publisher Site

Abstract

The crystal structure of the haematopoietic cell kinase Hck has been determined at 2.6/2.9 Å 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.

Journal

NatureSpringer Journals

Published: Feb 13, 1997

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