Biomolecular NMR Assignments

, Volume 8, Issue 2, pp 297–301 | Cite as

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

  • Lucia Rubio
  • Radu Huculeci
  • Lieven Buts
  • Sophie Vanwetswinkel
  • Tom Lenaerts
  • Nico A. J. van Nuland
Article

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 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.

Keywords

SH2 domain Macromolecular complex NMR Shp2 PTPN11 Erythropoietin receptor 

Notes

Acknowledgments

This work received financial support from the VIB, FWO-Vlaanderen, the Onderzoeksfonds of the Vrije Universiteit Brussel (OZR-VUB) and the Hercules Foundation. This work is also supported by FWO grant G.0116.09 N.

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Copyright information

© Springer Science+Business Media Dordrecht 2013

Authors and Affiliations

  • Lucia Rubio
    • 1
    • 2
  • Radu Huculeci
    • 1
    • 2
  • Lieven Buts
    • 1
    • 2
  • Sophie Vanwetswinkel
    • 1
    • 2
  • Tom Lenaerts
    • 3
    • 4
  • Nico A. J. van Nuland
    • 1
    • 2
  1. 1.Jean Jeener NMR Centre, Structural Biology BrusselsVrije Universiteit BrusselBrusselsBelgium
  2. 2.Molecular Recognition Unit, Department of Structural BiologyVIBBrusselsBelgium
  3. 3.MLG, Département d’informatiqueUniversité Libre de BruxellesBrusselsBelgium
  4. 4.AI-lab, Vakgroep ComputerwetenschappenVrije Universiteit BrusselBrusselsBelgium

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