Huculeci Radu, Buts Lieven, Lenaerts Tom, van Nuland Nico A J
Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050, Brussel, Belgium.
Biomol NMR Assign. 2011 Oct;5(2):181-4. doi: 10.1007/s12104-011-9295-4. Epub 2011 Feb 8.
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 (1)H, (15)N and (13)C 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.
SH2结构域是专门用于识别磷酸酪氨酸位点的相互作用模块,在例如酪氨酸激酶或磷酸酶的激活中发挥核心作用。本文报道了人蛋白酪氨酸激酶Fyn的SH2结构域在游离状态以及与对应于仓鼠中T抗原特定序列的高亲和力磷酸酪氨酸肽结合时的(1)H、(15)N和(13)C主链及侧链化学位移归属。BMRB登录号分别为17368和17369。