Jacob, Sandra (2006) Structural biology of protein tyrosine kinases. Cellular and Molecular Life Sciences : CMLS, 63 (22). pp. 2608-2625. ISSN 1420-682X

Abstract

Our current understanding of the structure, mechanism of action and modes of regulation of the protein tyrosine kinase family owes a great deal to structural biology. Structures are now available for more than 20 different tyrosine kinase domains, many of these in multiple conformational states. They form the basis for the design of experiments to further investigate the role of different structural elements in the normal function and regulation of the protein and in the pathogenesis of many human diseases. Once thought to be too similar to be specifically inhibited by a small molecule, structural differences between kinases allow the design of compounds which inhibit only an acceptable few. This review gives a general overview of protein tyrosine kinase structural biology, including a discussion of the strengths and limitations of the investigative methods involved.

Item Type:	Article
Related URLs:	http://www.ncbi.nlm.nih.gov/sites/entrez...
Additional Information:	author can archive post-print (ie final draft post-refereeing); Publisher's version/PDF cannot be used
Keywords:	Kinase structure; structural biology; protein crystallography; protein nuclear magnetic resonance spectroscopy; conformational flexibility; regulatory domain; drug discovery
Related URLs:	http://www.ncbi.nlm.nih.gov/sites/entrez...
Date Deposited:	14 Dec 2009 13:57
Last Modified:	31 Jan 2013 01:13
URI:	https://oak.novartis.com/id/eprint/583