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Article
Murine Itk SH3 domain
Journal of Biomolecular NMR
  • Andrew Severin, Iowa State University
  • D. Bruce Fulton, Iowa State University
  • Amy H. Andreotti, Iowa State University
Document Type
Article
Publication Version
Accepted Manuscript
Publication Date
4-1-2008
DOI
10.1007/s10858-008-9231-9
Abstract

Interleukin-2 tyrosine kinase (Itk) is a non-receptor tyrosine kinase of the Tec family that is activated upon antigen binding to the T cell receptor (Schwartzberg et al. 2005; Berg 2007). Itk is comprised of four regulatory domains: PH (Pleckstrin homology), TH (Tec homology), SH3, SH2 and the catalytic kinase domain. SH3 domains share a common fold consisting of five anti-parallel β strands that form a β barrel and bind canonical proline rich ligands as well as a variety of noncanonical ligands (Agrawal and Kishan 2002).

Comments

This is a post-peer-review, pre-copyedit version of an article published in Journal of Biomolecular NMR. The final authenticated version is available online at: http://dx.doi.org/10.1007/s10858-008-9231-9.

Copyright Owner
Springer Science+Business Media B.V.
Language
en
File Format
application/pdf
Citation Information
Andrew Severin, D. Bruce Fulton and Amy H. Andreotti. "Murine Itk SH3 domain" Journal of Biomolecular NMR Vol. 40 Iss. 4 (2008) p. 285 - 290
Available at: http://works.bepress.com/amy_andreotti/22/