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(1)H, (13)C, and (15)N backbone and side-chain chemical shift assignments of the free and bound forms of the human PTPN11 second SH2 domain.

par Rubio, Lucia;Huculeci, Radu;Buts, Lieven;Vanwetswinkel, Sophie ;Lenaerts, Tom ;van Nuland, Nico A J
Référence Biomolecular N M R Assignments, 8, 297
Publication Publié, 2014-07-10

Article révisé par les pairs

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Résumé :

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 (1)H, (15)N and (13)C 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.