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1H, 15N and 13C backbone resonance assignments of the archetypal serpin ?1-antitrypsin.

ABSTRACT: Alpha(1)-antitrypsin is a 45-kDa (394-residue) serine protease inhibitor synthesized by hepatocytes, which is released into the circulatory system and protects the lung from the actions of neutrophil elastase via a conformational transition within a dynamic inhibitory mechanism. Relatively common point mutations subvert this transition, causing polymerisation of ?(1)-antitrypsin and deficiency of the circulating protein, predisposing carriers to severe lung and liver disease. We have assigned the backbone resonances of ?(1)-antitrypsin using multidimensional heteronuclear NMR spectroscopy. These assignments provide the starting point for a detailed solution state characterization of the structural properties of this highly dynamic protein via NMR methods.

SUBMITTER: Nyon MP

PROVIDER: S-EPMC3438405 | biostudies-literature | 2012 Oct

REPOSITORIES: biostudies-literature

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1H, 15N and 13C backbone resonance assignments of the archetypal serpin α1-antitrypsin.

Nyon Mun Peak MP Kirkpatrick John J Cabrita Lisa D LD Christodoulou John J Gooptu Bibek B

Biomolecular NMR assignments 20111123 2

Alpha(1)-antitrypsin is a 45-kDa (394-residue) serine protease inhibitor synthesized by hepatocytes, which is released into the circulatory system and protects the lung from the actions of neutrophil elastase via a conformational transition within a dynamic inhibitory mechanism. Relatively common point mutations subvert this transition, causing polymerisation of α(1)-antitrypsin and deficiency of the circulating protein, predisposing carriers to severe lung and liver disease. We have assigned th ...[more]

PMID: 22109101

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