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Backbone 1H, 13C, and 15N resonance assignments for the 26-kD human de-ubiquitinating enzyme UCH-L3

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Abstract

To facilitate NMR spectroscopy studies of interactions with various ligands and potential inhibitors, we report the NMR backbone resonance assignments for the 26 kD human enzyme UCH-L3, a member of the ubiquitin C-hydrolase family of ubiquitin-specific cysteine proteases.

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Acknowledgements

We acknowledge Dr Beatriz Simas Magalhaes for fruitful discussions of aspects of this work.

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Authors and Affiliations

  1. Department of Biochemistry and Molecular Biology, University College London, Darwin Building, Gower Street, London, WC1E 6BT, UK

    Richard Harris & Paul C. Driscoll

  2. Institute of Structural Molecular Biology, UCL/Birkbeck, Malet Street, London, WC1E 7HX, UK

    Richard Harris & Paul C. Driscoll

  3. Expertise Platform Proteases, Novartis Institutes for Biomedical Research, Basel, 4002, Switzerland

    Ulf Eidhoff, Daniela Vinzenz, Martin Renatus, Bernd Gerhartz & Ulrich Hommel

Authors
  1. Richard Harris
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  2. Ulf Eidhoff
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  3. Daniela Vinzenz
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  4. Martin Renatus
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  5. Bernd Gerhartz
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  6. Ulrich Hommel
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  7. Paul C. Driscoll
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Correspondence to Paul C. Driscoll.

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Harris, R., Eidhoff, U., Vinzenz, D. et al. Backbone 1H, 13C, and 15N resonance assignments for the 26-kD human de-ubiquitinating enzyme UCH-L3. Biomol NMR Assign 1, 51–53 (2007). https://doi.org/10.1007/s12104-007-9012-5

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  • DOI: https://doi.org/10.1007/s12104-007-9012-5

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