title: Complete 1H, 15N and 13C assignment of trappin-2 and 1H assignment of its two domains, elafin and cementoin.
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 (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.
authors.affiliation: 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.
authors.forename: Karine
authors.initials: K
authors.lastname: Loth
authors.affiliation: Centre de Biophysique Moléculaire, Centre National de la Recherche Scientifique (CNRS) UPR 4301, Université d'Orléans, rue Charles Sadron, 45071, Orléans Cedex 2, France.
authors.forename: Soha Abou Ibrahim
authors.initials: SA
authors.lastname: Alami
authors.affiliation: Centre de Biophysique Moléculaire, Centre National de la Recherche Scientifique (CNRS) UPR 4301, Université d'Orléans, rue Charles Sadron, 45071, Orléans Cedex 2, France.
authors.forename: Chahrazed
authors.initials: C
authors.lastname: Habès
authors.affiliation: Pathologies Respiratoires: Protéolyse et Aérosolthérapie, Faculté de Médecine, INSERM U1100, 10 Bd Tonnellé, 37032, Tours Cedex, France.
authors.forename: Solène
authors.initials: S
authors.lastname: Garrido
authors.affiliation: Centre de Biophysique Moléculaire, Centre National de la Recherche Scientifique (CNRS) UPR 4301, Université d'Orléans, rue Charles Sadron, 45071, Orléans Cedex 2, France.
authors.forename: Vincent
authors.initials: V
authors.lastname: Aucagne
authors.affiliation: Centre de Biophysique Moléculaire, Centre National de la Recherche Scientifique (CNRS) UPR 4301, Université d'Orléans, rue Charles Sadron, 45071, Orléans Cedex 2, France.
authors.forename: Agnès F
authors.initials: AF
authors.lastname: Delmas
authors.affiliation: Pathologies Respiratoires: Protéolyse et Aérosolthérapie, Faculté de Médecine, INSERM U1100, 10 Bd Tonnellé, 37032, Tours Cedex, France.
authors.forename: Thierry
authors.initials: T
authors.lastname: Moreau
authors.affiliation: Pathologies Respiratoires: Protéolyse et Aérosolthérapie, Faculté de Médecine, INSERM U1100, 10 Bd Tonnellé, 37032, Tours Cedex, France.
authors.forename: Marie-Louise
authors.initials: ML
authors.lastname: Zani
authors.affiliation: Centre de Biophysique Moléculaire, Centre National de la Recherche Scientifique (CNRS) UPR 4301, Université d'Orléans, rue Charles Sadron, 45071, Orléans Cedex 2, France.
authors.forename: Céline
authors.initials: C
authors.lastname: Landon
mesh_terms: D000595:Amino Acid Sequence; D053492:Elafin / Q000737:chemistry*; D006801:Humans; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry*; D000072417:Protein Domains
chemical_list: D053492:Elafin; C506806:PI3 protein, human; D010455:Peptides; C088842:cementoin
keywords: Cementoin; Elafin; Inflammatory lung diseases; Protease inhibitor; Serine proteases; Trappin-2