Accueil > Publications > Recherche par années > Années 2010 > 2016

Loth K., Alami S. A. I., Habès C., Garrido S., Aucagne V., Delmas A.F., Moreau, T., Zani M.-L. and Landon C.

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

Biomolecular NMR Assignments (2016) 10 (1) 223-226 - doi : 10.1007/s12104-016-9671-1

par Frapart - publié le , mis à jour le

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.