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Complete 1H, 15N and 13C assignment of trappin-2 and 1H assignment of its two domains, elafin and cementoin

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Abstract

Trappin-2 is a serine protease inhibitor with a very narrow inhibitory spectrum and has significant anti-microbial activities. It is a 10 kDa cationic protein composed of two distinct domains. The N-terminal domain (38 residues) named cementoin is known to be intrinsically disordered when it is not linked to the elafin. The C-terminal domain (57 residues), corresponding to elafin, is a cysteine-rich domain stabilized by four disulfide bridges and is characterized by a flat core and a flexible N-terminal part. To our knowledge, there is no structural data available on trappin-2. We report here the complete 1H, 15N and 13C resonance assignment of the recombinant trappin-2 and the 1H assignments of cementoin and elafin, under the same experimental conditions. This is the first step towards the 3D structure determination of the trappin-2.

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Acknowledgments

This work was supported by the committees of the Région Centre-Val de Loire (TRAP2VEC project). We thank Philippe Marceau for support for solid phase peptide synthesis.

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Authors and Affiliations

  1. Centre de Biophysique Moléculaire, Centre National de la Recherche Scientifique (CNRS) UPR 4301, Université d’Orléans, rue Charles Sadron, 45071, Orléans Cedex 2, France

    Karine Loth, Soha Abou Ibrahim Alami, Chahrazed Habès, Vincent Aucagne, Agnès F. Delmas & Céline Landon

  2. Pathologies Respiratoires: Protéolyse et Aérosolthérapie, Faculté de Médecine, INSERM U1100, 10 Bd Tonnellé, 37032, Tours Cedex, France

    Solène Garrido, Thierry Moreau & Marie-Louise Zani

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  1. Karine Loth
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  2. Soha Abou Ibrahim Alami
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  3. Chahrazed Habès
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  4. Solène Garrido
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  5. Vincent Aucagne
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  6. Agnès F. Delmas
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  7. Thierry Moreau
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  8. Marie-Louise Zani
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  9. Céline Landon
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Correspondence to Karine Loth.

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Loth, K., Alami, S.A.I., Habès, C. et al. Complete 1H, 15N and 13C assignment of trappin-2 and 1H assignment of its two domains, elafin and cementoin. Biomol NMR Assign 10, 223–226 (2016). https://doi.org/10.1007/s12104-016-9671-1

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  • DOI: https://doi.org/10.1007/s12104-016-9671-1

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