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 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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https://hal.archives-ouvertes.fr/hal-01407495
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Submitted on : Friday, December 2, 2016 - 11:46:32 AM
Last modification on : Friday, July 12, 2019 - 1:29:18 AM

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Karine Loth, Soha Abou Ibrahim Alami, Chahrazed Habès, Solène Garrido, Vincent Aucagne, et al.. Complete 1H, 15N and 13C assignment of trappin-2 and 1H assignment of its two domains, elafin and cementoin. Biomolecular NMR Assignments, Springer, 2016, 10 (1), pp.223 - 226. ⟨10.1007/s12104-016-9671-1⟩. ⟨hal-01407495⟩

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