Document Type

Article

Publication Version

Published Version

Publication Date

2-2011

Journal or Book Title

Acta Crystallographica Section F

Volume

67

Issue

2

First Page

269

Last Page

273

DOI

10.1107/S1744309110052346

Abstract

Proline is a unique amino acid owing to the relatively small energy difference between the cis and trans conformations of its peptide bond. The X–Pro imide bond readily undergoes cistrans isomerization in the context of short peptides as well as some proteins. However, the direct detection of cistrans proline isomerization in folded proteins is technically challenging. NMR spectroscopy is well suited to the direct detection of proline isomerization in folded proteins. It is less clear how well X-ray crystallography can reveal this conformational exchange event in folded proteins. Conformational heterogeneity owing to cistrans proline isomerization in the Src homology 2 (SH2) domain of the IL-2-inducible T-cell kinase (ITK) has been extensively characterized by NMR. Using the ITK SH2 domain as a test system, an attempt was made to determine whether proline isomerization could be detected in a crystal structure of the ITK SH2 domain. As a first step towards this goal, the purification, crystallization and preliminary characterization of the ITK SH2 domain are described.

Comments

This article is from Acta Crystallographica Section F 67 (2011): 269, doi:10.1107/S1744309110052346.

Rights

Works produced by employees of the U.S. Government as part of their official duties are not copyrighted within the U.S. The content of this document is not copyrighted.

Language

en

File Format

application/pdf

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