1H, 13C, and 15N backbone and side-chain chemical shift assignments of the free and bound forms of the human PTPN11 second SH2 domain
Src homology 2 (SH2) domains have an important role in the regulation of protein activity and intracellular signaling processes. They are geared to bind to specific phosphotyrosine (pY) motifs, with a substrate sequence specificity depending on the three amino acids immediately C-terminal to the pY. Here we report for the first time the 1H, 15N and 13C backbone and side-chain chemical shift assignments for the C-terminal SH2 domain of the human protein tyrosine phosphatase PTPN11, both in its free and bound forms, where the ligand in the latter corresponds to a specific sequence of the human erythropoietin receptor.
KeywordsSH2 domain Macromolecular complex NMR Shp2 PTPN11 Erythropoietin receptor
This work received financial support from the VIB, FWO-Vlaanderen, the Onderzoeksfonds of the Vrije Universiteit Brussel (OZR-VUB) and the Hercules Foundation. This work is also supported by FWO grant G.0116.09 N.
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