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

M.P. Nyon; J. Kirkpatrick; L.D. Cabrita; J. Christodoulou; Bibekbrata Gooptu

doi:10.1007/s12104-011-9345-y

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

M.P. Nyon, J. Kirkpatrick, L.D. Cabrita, J. Christodoulou, Bibekbrata Gooptu

Research output: Contribution to journal › Article › peer-review

6 Citations (Scopus)

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.

Original language	English
Pages (from-to)	153-156
Number of pages	4
Journal	Biomolecular NMR Assignments
Volume	6
Issue number	2
DOIs	https://doi.org/10.1007/s12104-011-9345-y
Publication status	Published - Oct 2012

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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.",

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AU - Nyon, M.P.

AU - Kirkpatrick, J.

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AU - Christodoulou, J.

AU - Gooptu, Bibekbrata

PY - 2012/10

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AB - 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.

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

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