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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.

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 TypeJournal Article
Year of Publication2013
AuthorsRubio, L, Huculeci, R, Buts, L, Vanwetswinkel, S, Lenaerts, T, van Nuland, NAJ
JournalAdvances in hematology
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.

URLhttp://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/155960

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