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

• Published in: Biomolecular NMR assignments Vol. 8; no. 2; p. 297
• Main Authors: Rubio, Lucia, Huculeci, Radu, Buts, Lieven, Vanwetswinkel, Sophie, Lenaerts, Tom, van Nuland, Nico A; J
• Format: Journal Article
• Language: English
• Published: Dordrecht Springer Nature B.V 01.10.2014
• Subjects: Amino acids; NMR; Nuclear magnetic resonance; Phosphatase; Proteins; Signal transduction
• DOI: 10.1007/s12104-013-9504-4
• ISSN: 1874-2718

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 ^sup 1^H, ^sup 15^N and ^sup 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.[PUBLICATION ABSTRACT]