sup 1^H, ^sup 15^N and ^sup 13^C backbone resonance assignments of the archetypal serpin [alpha]^sub 1^-antitrypsin

Alpha^sub 1^-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 commo...

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Bibliographic Details
Published in:Biomolecular NMR assignments 2012-10, Vol.6 (2), p.153
Main Authors: Nyon, Mun Peak, Kirkpatrick, John, Cabrita, Lisa D, Christodoulou, John, Gooptu, Bibek
Format: Article
Language:English
Subjects:
Glycoproteins
NMR
Nuclear magnetic resonance
Protease inhibitors
Protein folding
Online Access:Get full text
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Summary:Alpha^sub 1^-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 α^sub 1^-antitrypsin and deficiency of the circulating protein, predisposing carriers to severe lung and liver disease. We have assigned the backbone resonances of α^sub 1^-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.[PUBLICATION ABSTRACT]
ISSN:1874-2718
1874-270X
DOI:10.1007/s12104-011-9345-y