Biomolecular NMR Assignments

, Volume 5, Issue 2, pp 181–184

1H, 13C and 15N backbone and side-chain chemical shift assignment of the Fyn SH2 domain and its complex with a phosphotyrosine peptide

  • Radu Huculeci
  • Lieven Buts
  • Tom Lenaerts
  • Nico A. J. van Nuland
Article

DOI: 10.1007/s12104-011-9295-4

Cite this article as:
Huculeci, R., Buts, L., Lenaerts, T. et al. Biomol NMR Assign (2011) 5: 181. doi:10.1007/s12104-011-9295-4

Abstract

SH2 domains are interaction modules uniquely dedicated to recognize phosphotyrosine sites, playing a central role in for instance the activation of tyrosine kinases or phosphatases. Here we report the 1H, 15N and 13C backbone and side-chain chemical shift assignments of the SH2 domain of the human protein tyrosine kinase Fyn, both in its free state and bound to a high-affinity phosphotyrosine peptide corresponding to a specific sequence in the hamster middle-T antigen. The BMRB accession numbers are 17,368 and 17,369, respectively.

Keywords

SH2 domain Macromolecular complex NMR Fyn Src kinase 

Copyright information

© Springer Science+Business Media B.V. 2011

Authors and Affiliations

  • Radu Huculeci
    • 1
    • 2
  • Lieven Buts
    • 1
    • 2
  • Tom Lenaerts
    • 3
    • 4
  • Nico A. J. van Nuland
    • 1
    • 2
  1. 1.Structural Biology BrusselsVrije Universiteit BrusselBrusselBelgium
  2. 2.Department of Molecular and Cellular InteractionsVIBBrusselBelgium
  3. 3.MLG, Département d’informatiqueUniversité Libre de BruxellesBrusselBelgium
  4. 4.AI-lab, Vakgroep ComputerwetenschappenVrije Universiteit BrusselBrusselBelgium

Personalised recommendations