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

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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 1H, 15N and 13C 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.
Tijdschrift: Biomol. NMR Assign.
ISSN: 1874-2718
Volume: 8
Pagina's: 297-301
Jaar van publicatie:2014
Trefwoorden:SH2 domains, Macromolecular recognition, Shp2, NMR
  • ORCID: /0000-0003-3645-1455/work/71346871
  • Scopus Id: 84879774446