1H, 13C and 15N backbone and side-chain chemical shift assignment of the Fyn SH2 domain and its complex with a phosphotyrosine peptide

被引：0
|
作者：
Radu Huculeci
Lieven Buts
Tom Lenaerts
Nico A. J. van Nuland
机构：
[1] Vrije Universiteit Brussel,Structural Biology Brussels
[2] VIB,Department of Molecular and Cellular Interactions
[3] Université Libre de Bruxelles,MLG, Département d’informatique
[4] Vrije Universiteit Brussel,AI
来源：
Biomolecular NMR Assignments | 2011年 / 5卷
关键词：
SH2 domain; Macromolecular complex; NMR; Fyn; Src kinase;
D O I：
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中图分类号：
学科分类号：
摘要：
SH2 domains are interaction modules uniquely dedicated to recognize phosphotyrosine sites, playing a central role in for instance the activation of tyrosine kinases or phosphatases. Here we report the 1H, 15N and 13C backbone and side-chain chemical shift assignments of the SH2 domain of the human protein tyrosine kinase Fyn, both in its free state and bound to a high-affinity phosphotyrosine peptide corresponding to a specific sequence in the hamster middle-T antigen. The BMRB accession numbers are 17,368 and 17,369, respectively.
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页码：181 / 184
页数：3
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