Inhibitory conformation of the reactive loop of alpha 1-antitrypsin.
Nat Struct Biol
; 3(8): 676-81, 1996 Aug.
Article
em En
| MEDLINE
| ID: mdl-8756325
ABSTRACT
The reactive site loop of the serpin family of serine proteinase inhibitors is flexible and can adopt a number of diverse conformations. A 2.9 A resolution structure of alpha 1-antitrypsin-the principal proteinase inhibitor in human plasma-shows the loop in a stable canonical conformation matching that found in all other families of serine proteinase inhibitors. This unexpected finding in the absence of loop insertion into the body of the molecule favours a two-stage mechanism of inhibition and provides a model for the heparin activation of antithrombin. The beta-pleated strand conformation of the loop also accounts for the polymerization of the serpins in disease and for their association with other beta-sheet structures, most notably the beta-amyloid of Alzheimer's disease.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Alfa 1-Antitripsina
Tipo de estudo:
Etiology_studies
/
Prognostic_studies
Limite:
Humans
Idioma:
En
Revista:
Nat Struct Biol
Assunto da revista:
BIOLOGIA MOLECULAR
Ano de publicação:
1996
Tipo de documento:
Article
País de afiliação:
Reino Unido