1H, 15N and 13C backbone resonance assignments of the archetypal serpin α1-antitrypsin
Nyon, Mun Peak and Kirkpatrick, J. and Cabrita, L.D. and Christodoulou, John and Gooptu, Bibek (2012) 1H, 15N and 13C backbone resonance assignments of the archetypal serpin α1-antitrypsin. Biomolecular NMR Assignments 6 (2), pp. 153-156. ISSN 1874-2718.
Alpha1-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 α1-antitrypsin and deficiency of the circulating protein, predisposing carriers to severe lung and liver disease. We have assigned the backbone resonances of α1-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.
|Keyword(s) / Subject(s):||Serpin, Antitrypsin, Assignment, Refolding|
|School:||Birkbeck Schools and Departments > School of Science > Biological Sciences|
|Research Centre:||Structural Molecular Biology, Institute of (ISMB)|
|Date Deposited:||16 Jan 2012 15:04|
|Last Modified:||06 Dec 2016 10:42|
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