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1H, 13C and 15N resonance assignments of the Onconase FL-G zymogen

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Abstract

Onconase® FL-G zymogen is a 120 residue protein produced by circular permutation of the native Onconase® sequence. In this construction, the wild type N- and C-termini are linked by a 16 residue segment and new N- and C-termini are generated at wild type positions R73 and S72. This novel segment linking the native N- and C-termini is designed to obstruct Onconase’s® active site and encloses a cleavage site for the HIV-1 protease. As a first step towards the resolution of its 3D structure and the study of its structure–function relationships, we report here the nearly complete NMR 1H, 13C and 15N resonance chemical shift assignments at pH 5.2 and 35°C (BMRB deposit no 17973). The results presented here clearly show that the structure of the wild type Onconase® is conserved in the FL-G zymogen.

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Acknowledgements

This work was supported by the projects, CTQ2008-0080, CTQ2010-21567-C02-02 and BFU2009-06935/BMC from MICINN and PUG2008A from the Universitat de Girona. MC acknowledges a fellowship from Ministerio de Educación y Ciencia.

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Authors and Affiliations

  1. Instituto de Química Física “Rocasolano”, Consejo Superior de Investigaciones Científicas, Serrano 119, 28006, Madrid, Spain

    Soraya Serrano, Douglas V. Laurents & Marta Bruix

  2. Laboratori d’Enginyeria de Proteïnes, Departament de Biologia, Facultat de Ciències, Universitat de Girona, Maria Aurèlia Capmany 69, 17071, Girona, Spain

    Mariona Callís, Maria Vilanova, Antoni Benito & Marc Ribó

Authors
  1. Soraya Serrano
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  2. Mariona Callís
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  3. Maria Vilanova
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  4. Antoni Benito
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  5. Douglas V. Laurents
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  6. Marc Ribó
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  7. Marta Bruix
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Corresponding authors

Correspondence to Marc Ribó or Marta Bruix.

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Serrano, S., Callís, M., Vilanova, M. et al. 1H, 13C and 15N resonance assignments of the Onconase FL-G zymogen. Biomol NMR Assign 7, 13–15 (2013). https://doi.org/10.1007/s12104-012-9367-0

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  • DOI: https://doi.org/10.1007/s12104-012-9367-0

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