title: 1H, 15N and 13C backbone resonance assignments of the archetypal serpin α1-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 α(1)-antitrypsin and deficiency of the circulating protein, predisposing carriers to severe lung and liver disease. We have assigned the backbone resonances of α(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.
authors: Department of Biological Sciences, Institute of Structural and Molecular Biology, Crystallography, Birkbeck College, University of London, Malet Street, London WC1E 7HX, UK.
authors: Mun Peak
authors: MP
authors: Nyon
authors: John
authors: J
authors: Kirkpatrick
authors: Lisa D
authors: LD
authors: Cabrita
authors: John
authors: J
authors: Christodoulou
authors: Bibek
authors: B
authors: Gooptu
mesh_terms: D000595:Amino Acid Sequence; D002247:Carbon Isotopes; D006801:Humans; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D011522:Protons; D000515:alpha 1-Antitrypsin / Q000737:chemistry*
chemical_list: D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D011522:Protons; D000515:alpha 1-Antitrypsin