1H, 15N and 13C backbone resonance assignments of the archetypal serpin α1-antitrypsinReport as inadecuate




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Biomolecular NMR Assignments

, Volume 6, Issue 2, pp 153–156

First Online: 23 November 2011Received: 11 August 2011Accepted: 02 November 2011

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. 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.

KeywordsSerpin Antitrypsin Assignment Refolding M. P. Nyon, J. Kirkpatrick contributed equally.

Electronic supplementary materialThe online version of this article doi:10.1007-s12104-011-9345-y contains supplementary material, which is available to authorized users.

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Author: Mun Peak Nyon - John Kirkpatrick - Lisa D. Cabrita - John Christodoulou - Bibek Gooptu

Source: https://link.springer.com/







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