期刊
BIOMOLECULAR NMR ASSIGNMENTS
卷 6, 期 2, 页码 153-156出版社
SPRINGER
DOI: 10.1007/s12104-011-9345-y
关键词
Serpin; Antitrypsin; Assignment; Refolding
资金
- Wellcome Trust
- Medical Research Council (UK)
- Human Frontiers Science Programme
- Biotechnology and Biological Sciences Research Council
- Papworth Hospital NHS Trust
- Birkbeck College Faculty Research Fund
- Medical Research Council [MC_U117533887] Funding Source: researchfish
- MRC [MC_U117533887] Funding Source: UKRI
Alpha(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 alpha(1)-antitrypsin and deficiency of the circulating protein, predisposing carriers to severe lung and liver disease. We have assigned the backbone resonances of alpha(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.
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