Unknown

Dataset Information

0

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

ABSTRACT: 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 ?(1)-antitrypsin and deficiency of the circulating protein, predisposing carriers to severe lung and liver disease. We have assigned the backbone resonances of ?(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.

SUBMITTER: Nyon MP 

PROVIDER: S-EPMC3438405 | biostudies-literature | 2012 Oct

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

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

Nyon Mun Peak MP   Kirkpatrick John J   Cabrita Lisa D LD   Christodoulou John J   Gooptu Bibek B  

Biomolecular NMR assignments 20111123 2

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 α(1)-antitrypsin and deficiency of the circulating protein, predisposing carriers to severe lung and liver disease. We have assigned th  ...[more]

Similar Datasets

Unknown Backbone 1H, 13C and 15N resonance assignments of the extracellular domain of tissue factor.
| S-EPMC2947601 | biostudies-literature
Unknown 1H, 15N and 13C backbone resonance assignments of pentaerythritol tetranitrate reductase from Enterobacter cloacae PB2.
| S-EPMC5869876 | biostudies-literature
Unknown 1H, 13C, and 15N backbone and side chain resonance assignments of thermophilic Geobacillus kaustophilus cyclophilin-A.
| S-EPMC4084936 | biostudies-literature
Unknown Sequence-specific 1H, 13C and 15N backbone resonance assignments of the plakin repeat domain of human envoplakin.
| S-EPMC4788679 | biostudies-literature
Unknown 1H, 13C and 15N resonance assignments of the Calmodulin-Munc13-1 peptide complex.
| S-EPMC2862173 | biostudies-literature
Unknown 1H, 13C and 15N backbone resonance assignment of BRCA1 fragment 219-504.
| S-EPMC7462910 | biostudies-literature
Unknown 1H, 15N and 13C backbone resonance assignments of the P146A variant of ?-phosphoglucomutase from Lactococcus lactis in its substrate-free form.
| S-EPMC6713671 | biostudies-literature
Unknown 1H, 13C and 15N resonance assignments of SARS-CoV main protease N-terminal domain.
| S-EPMC7091140 | biostudies-literature
Unknown 1H, 13C, and 15N chemical shift assignments of ZCCHC9.
| S-EPMC3049224 | biostudies-literature
Unknown Sequence-specific 1H N, 13C, and 15N backbone resonance assignments of the 34 kDa Paramecium bursaria Chlorella virus 1 (PBCV1) DNA ligase.
| S-EPMC2746884 | biostudies-literature