title: ¹H, ¹³C and ¹⁵N backbone and side-chain chemical shift assignments of the free and bound forms of the human PTPN11 second SH2 domain.
abstract: 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.
authors.affiliation: Jean Jeener NMR Centre, Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050, Brussels, Belgium.
authors.forename: Lucia
authors.initials: L
authors.lastname: Rubio
authors.forename: Radu
authors.initials: R
authors.lastname: Huculeci
authors.forename: Lieven
authors.initials: L
authors.lastname: Buts
authors.forename: Sophie
authors.initials: S
authors.lastname: Vanwetswinkel
authors.forename: Tom
authors.initials: T
authors.lastname: Lenaerts
authors.forename: Nico A J
authors.initials: NA
authors.lastname: van Nuland
mesh_terms: D000595:Amino Acid Sequence; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D010446:Peptide Fragments / Q000378:metabolism; D011485:Protein Binding; D054592:Protein Tyrosine Phosphatase, Non-Receptor Type 11 / Q000737:chemistry* / Q000378:metabolism*; D018909:src Homology Domains
chemical_list: D010446:Peptide Fragments; D054592:Protein Tyrosine Phosphatase, Non-Receptor Type 11