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

Autor: Loth K; 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@cnrs-orleans.fr., Alami SA; Centre de Biophysique Moléculaire, Centre National de la Recherche Scientifique (CNRS) UPR 4301, Université d'Orléans, rue Charles Sadron, 45071, Orléans Cedex 2, France., Habès C; Centre de Biophysique Moléculaire, Centre National de la Recherche Scientifique (CNRS) UPR 4301, Université d'Orléans, rue Charles Sadron, 45071, Orléans Cedex 2, France., Garrido S; Pathologies Respiratoires: Protéolyse et Aérosolthérapie, Faculté de Médecine, INSERM U1100, 10 Bd Tonnellé, 37032, Tours Cedex, France., Aucagne V; Centre de Biophysique Moléculaire, Centre National de la Recherche Scientifique (CNRS) UPR 4301, Université d'Orléans, rue Charles Sadron, 45071, Orléans Cedex 2, France., Delmas AF; Centre de Biophysique Moléculaire, Centre National de la Recherche Scientifique (CNRS) UPR 4301, Université d'Orléans, rue Charles Sadron, 45071, Orléans Cedex 2, France., Moreau T; Pathologies Respiratoires: Protéolyse et Aérosolthérapie, Faculté de Médecine, INSERM U1100, 10 Bd Tonnellé, 37032, Tours Cedex, France., Zani ML; Pathologies Respiratoires: Protéolyse et Aérosolthérapie, Faculté de Médecine, INSERM U1100, 10 Bd Tonnellé, 37032, Tours Cedex, France., Landon C; Centre de Biophysique Moléculaire, Centre National de la Recherche Scientifique (CNRS) UPR 4301, Université d'Orléans, rue Charles Sadron, 45071, Orléans Cedex 2, France.
Jazyk: angličtina
Zdroj: Biomolecular NMR assignments [Biomol NMR Assign] 2016 Apr; Vol. 10 (1), pp. 223-6. Date of Electronic Publication: 2016 Feb 15.
DOI: 10.1007/s12104-016-9671-1
Abstrakt: 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 (1)H, (15)N and (13)C resonance assignment of the recombinant trappin-2 and the (1)H assignments of cementoin and elafin, under the same experimental conditions. This is the first step towards the 3D structure determination of the trappin-2.
Databáze: MEDLINE
Externí odkaz: