Biomolecular NMR Assignments

, Volume 5, Issue 2, pp 181–184 | Cite as

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 NulandEmail author


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.


SH2 domain Macromolecular complex NMR Fyn Src kinase 



LB is a post-doctoral fellow of the F·W.O.-Vlaanderen. This work is supported by FWO grant G.0116.09 N and by grants from OZR-VUB and VIB.


  1. Arold ST, Ulmer TS, Mulhern TD, Werner JM, Ladbury JE, Campbell ID, Noble ME (2001) The role of the Src homology 3-Src homology 2 interface in the regulation of Src kinases. J Biol Chem 276:17199–17205CrossRefGoogle Scholar
  2. Bradshaw JM, Grucza RA, Ladbury JE, Waksman G (1998) Probing the “two-pronged plug two-holed socket” model for the mechanism of binding of the Src SH2 domain to phosphotyrosyl peptides: a thermodynamic study. Biochemistry 37:9083–9090CrossRefGoogle Scholar
  3. Chen Y, Delaglio F, Cornilescu G, Bax A (2009) TALOS plus: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J Biomol NMR 44:213–223CrossRefGoogle Scholar
  4. Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfiefer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277–293CrossRefGoogle Scholar
  5. Liu BA, Jablonowski K, Raina M, Arce M, Pawson T, Nash PD (2006) The human and mouse complement of SH2 domain proteins establishing the boundaries of phosphotyrosine signaling. Mol Cell 22:851–868CrossRefGoogle Scholar
  6. Machida K, Mayer BJ (2005) The SH2 domain: versatile signaling module and pharmaceutical target. Biochim Biophys Acta 1747:1–25Google Scholar
  7. Mulhern TD, Shaw GL, Morton CJ, Day AJ, Campbell ID (1997) The SH2 domain from the tyrosine kinase Fyn in complex with a phosphotyrosyl peptide reveals insights into domain stability and binding specificity. Structure 5:1313–1323CrossRefGoogle Scholar
  8. Pawson T (2004) Specificity in signal transduction: from phosphotyrosine-SH2 domain interactions to complex cellular systems. Cell 116:191–203CrossRefGoogle Scholar
  9. Pintar A, Hensmann M, Jumel K, Pitkeathly M, Harding SE, Campbell ID (1996) Solution studies of the SH2 domain from the Fyn tyrosine kinase: secondary structure, backbone dynamics and protein association. Eur Biophys J 24:371–380CrossRefGoogle Scholar
  10. Sattler M, Schleucher J, Griesinger C (1999) Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients. Prog Nucl Magn Reson Spectrosc 34:93–158CrossRefGoogle Scholar
  11. Schlessinger J, Lemmon MA (2003) SH2 and PTB domains in tyrosine kinase signaling. Sci STKE 191:RE12Google Scholar
  12. Suzuki M, Rohini R, Zheng H, Woychik NA, Inouye M (2006) Bacterial bioreactors for high yield production of recombinant protein. J Biol Chem 281:37559–37565CrossRefGoogle Scholar
  13. Vranken WF, Boucher W, Stevens TJ, Fogh RH, Pajon A, Llinas M, Ulrich EL, Markley JL, Ionides J, Laue ED (2005) The CCPN data model for NMR spectroscopy: development of a software pipeline. Proteins 59:687–696CrossRefGoogle Scholar
  14. Wishart DS, Sykes BD (1994) The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J Biomol NMR 4:171–180CrossRefGoogle Scholar
  15. Yamazaki T, Forman-Kay JD, Kay LE (1993) Two-dimensional NMR experiments for correlating 13Cb and 1Hd/e chemical shifts of aromatic residues in 13C-labeled proteins via scalar couplings. J Am Chem Soc 115:11054–11055CrossRefGoogle Scholar

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
    Email author
  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

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