ARTICLE 1H, 15N and 13C backbone resonance assignments of the archetypal serpin a1-antitrypsin

Abstract 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. Rela-tively common point mutations subvert this transition, causing polymerisation of a1-antitrypsin and deficiency of the circulating protein, predisposing carriers to severe lung and liver disease. We have assigned the backbone reso-nances of a1-antitrypsin using multidimensional heteronu-clear 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