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：1
|
作者：
Huculeci, Radu [1 ,2 ]
Buts, Lieven [1 ,2 ]
Lenaerts, Tom [3 ,4 ]
van Nuland, Nico A. J. [1 ,2 ]
机构：
[1] Vrije Univ Brussel, B-1050 Brussels, Belgium
[2] VIB, Dept Mol & Cellular Interact, B-1050 Brussels, Belgium
[3] Univ Libre Bruxelles, MLG, Dept Informat, B-1050 Brussels, Belgium
[4] Vrije Univ Brussel, AI Lab, Vakgrp Comp Wetenschappen, B-1050 Brussels, Belgium
来源：
BIOMOLECULAR NMR ASSIGNMENTS | 2011年 / 5卷 / 02期
关键词：
SH2; domain; Macromolecular complex; NMR; Fyn; Src kinase; SECONDARY STRUCTURE; NMR EXPERIMENTS; PROTEINS; BINDING; MODEL;
D O I：
10.1007/s12104-011-9295-4
中图分类号：
Q6 [生物物理学];
学科分类号：
071011 ;
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 H-1, N-15 and C-13 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.
引用
收藏
页码：181 / 184
页数：4
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