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Sequence-specific backbone 1H, 13C and 15N assignments of the 34 kDa catalytic domain of PTPN5 (STEP)

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Abstract

PTPN5 is a protein tyrosine phosphatase that plays an integral role in regulating excitatory postsynaptic activity. The sequence-specific backbone assignments of the murine PTPN5 catalytic domain have been determined based on triple-resonance experiments using uniformly [2H,13C,15N]-labeled protein.

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Acknowledgments

We thank Dr. Paul Lombroso, Yale University, for providing PTPN5 DNA. We thank Dr. Michael Clarkson for critical reading of the manuscript. This work was supported by an American Cancer Society Research Scholar Grant (RSG-08-067-01-LIB) to R.P. 800 MHz NMR data were recorded at Brandeis University. This spectrometer was funded by the National Institutes of Health grant S10-RR017269.

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Authors and Affiliations

  1. Department of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, RI, 02903, USA

    Dana M. Francis & Wolfgang Peti

  2. Department of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, RI, 02903, USA

    Rebecca Page

  3. Department of Chemistry, Brown University, Providence, RI, 02912, USA

    Wolfgang Peti

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  1. Dana M. Francis
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  2. Rebecca Page
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  3. Wolfgang Peti
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Correspondence to Rebecca Page or Wolfgang Peti.

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Francis, D.M., Page, R. & Peti, W. Sequence-specific backbone 1H, 13C and 15N assignments of the 34 kDa catalytic domain of PTPN5 (STEP). Biomol NMR Assign 8, 185–188 (2014). https://doi.org/10.1007/s12104-013-9480-8

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  • DOI: https://doi.org/10.1007/s12104-013-9480-8

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