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

7 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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T1 - 1H, 15N and 13C backbone resonance assignments of the archetypal serpin α1-antitrypsin

AU - Nyon, M.P.

AU - Kirkpatrick, J.

AU - Cabrita, L.D.

AU - Christodoulou, J.

AU - Gooptu, Bibekbrata

PY - 2012/10

Y1 - 2012/10

N2 - 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.

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.

UR - https://www.scopus.com/pages/publications/84873190761

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DO - 10.1007/s12104-011-9345-y

M3 - Article

SN - 1874-2718

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EP - 156

JO - Biomolecular NMR Assignments

JF - Biomolecular NMR Assignments

IS - 2

ER -

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

Abstract

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