Skip to main content
SpringerLink
Log in

1H, 15N and 13C sequence specific backbone assignment of the vanadate inhibited hematopoietic tyrosine phosphatase

  • Article
  • Published:
Biomolecular NMR Assignments Aims and scope Submit manuscript

Abstract

The sequence-specific backbone assignment of hematopoietic protein tyrosine phosphatase (HePTP; PTPN7) in presence of vanadate has been determined, based on triple-resonance experiments using uniformly [13C,15N]-labeled protein. These assignments facilitate further studies of HePTP in the presence of inhibitors to target leukemia and provide further insights into the function of protein tyrosine phosphatases.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2

Similar content being viewed by others

References

  • Choy MS, Li Y, Machado LESF et al (2017) Conformational rigidity and protein dynamics at distinct timescales regulate PTP1B activity and allostery. Mol Cell 65:644–658.e5. Doi:10.1016/j.molcel.2017.01.014

    Article  Google Scholar 

  • Delaglio F, Grzesiek S, Vuister GW et al (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277–293

    Article  Google Scholar 

  • Francis DM, Różycki B, Koveal D et al (2011) Structural basis of p38α regulation by hematopoietic tyrosine phosphatase. Nat Chem Biol 7:916–924. Doi:10.1038/nchembio.707

    Article  Google Scholar 

  • Jeeves M, McClelland DM, Barr AJ, Overduin M (2008) Sequence-specific 1H, 13C and 15N backbone resonance assignments of the 34 kDa catalytic domain of human PTPN7. Biomol NMR Assign 2:101–103. Doi:10.1007/s12104-008-9095-7

    Article  Google Scholar 

  • Machado LESF, Shen TL, Page R, Peti W (2017) The KIM-family protein-tyrosine phosphatases use distinct reversible oxidation intermediates: intramolecular or intermolecular disulfide bond formation. J Biol Chem 292(21):8786–8796. doi:10.1074/jbc.M116.774174

    Article  Google Scholar 

  • Muñoz JJ, Tárrega C, Blanco-Aparicio C, Pulido R (2003) Differential interaction of the tyrosine phosphatases PTP-SL, STEP and HePTP with the mitogen-activated protein kinases ERK1/2 and p38alpha is determined by a kinase specificity sequence and influenced by reducing agents. Biochem J 372:193–201. Doi:10.1042/BJ20021941

    Article  Google Scholar 

  • Peti W, Page R (2007) Strategies to maximize heterologous protein expression in Escherichia coli with minimal cost. Protein Expr Purif 51:1–10. Doi:10.1016/j.pep.2006.06.024

    Article  Google Scholar 

  • Sergienko E, Xu J, Liu WH et al (2012) Inhibition of hematopoietic protein tyrosine phosphatase augments and prolongs ERK1/2 and p38 activation. ACS Chem Biol 7:367–377. Doi:10.1021/cb2004274

    Article  Google Scholar 

  • Vranken WF, Boucher W, Stevens TJ et al (2005) The CCPN data model for NMR spectroscopy: development of a software pipeline. Proteins 59:687–696. Doi:10.1002/prot.20449

    Article  Google Scholar 

  • Zanke B, Suzuki H, Kishihara K et al (1992) Cloning and expression of an inducible lymphoid-specific, protein tyrosine phosphatase (HePTPase). Eur J Immunol 22:235–239. Doi:10.1002/eji.1830220134

    Article  Google Scholar 

  • Zanke B, Squire J, Griesser H et al (1994) A hematopoietic protein tyrosine phosphatase (HePTP) gene that is amplified and overexpressed in myeloid malignancies maps to chromosome 1q32.1. Leukemia 8:236–244

    Google Scholar 

Download references

Acknowledgements

This work was supported by the American Diabetes Association Pathway to Stop Diabetes Grant 1-14-ACN-31 and a Brazil Initiative Brown University grant to WP and NIH R01GM098482 to RP.

Author information

Author notes

  1. Luciana E. S. F. Machado, Rebecca Page & Wolfgang Peti

    Present address: Department of Chemistry and Biochemistry, University of Arizona, Tucson, AZ, 85721, USA

Authors and Affiliations

  1. Department of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, RI, 02912, USA

    Luciana E. S. F. Machado & Wolfgang Peti

  2. Department of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, RI, 02912, USA

    Rebecca Page

Authors
  1. Luciana E. S. F. Machado
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Rebecca Page
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Wolfgang Peti
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Wolfgang Peti.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Machado, L.E.S.F., Page, R. & Peti, W. 1H, 15N and 13C sequence specific backbone assignment of the vanadate inhibited hematopoietic tyrosine phosphatase. Biomol NMR Assign 12, 5–9 (2018). https://doi.org/10.1007/s12104-017-9770-7

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s12104-017-9770-7

Keywords

Search

Navigation