1H, 13C and 15N backbone and side-chain chemical shift assignment of the Fyn SH2 domain and its complex with a phosphotyrosine peptide
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.
KeywordsSH2 domain Macromolecular complex NMR Fyn Src kinase
LB is a post-doctoral fellow of the F·W.O.-Vlaanderen. This work is supported by FWO grant G.0116.09 N and by grants from OZR-VUB and VIB.