|Title||(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.|
|Publication Type||Journal Article|
|Year of Publication||2013|
|Authors||Rubio, L., R. Huculeci, L. Buts, S. Vanwetswinkel, T. Lenaerts, and N. A. J. van Nuland|
|Journal||Biomol NMR Assign|
|Date Published||2013 Jul 10|
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.
|Alternate Journal||Biomol NMR Assign|