Campus Units

Biochemistry, Biophysics and Molecular Biology, Roy J. Carver Department of

Document Type

Article

Publication Version

Accepted Manuscript

Publication Date

4-2008

Journal or Book Title

Journal of Biomolecular NMR

Volume

40

Issue

4

First Page

285

Last Page

290

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

Published Version

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