Inhibitory conformation of the reactive loop of alpha(1)-antitrypsin

Elliott, Peter R. and Lomas, David A. and Carrell, Robin W. and Abrahams, Jan Pieter. (1996) Inhibitory conformation of the reactive loop of alpha(1)-antitrypsin. Nature Structural biology, 3 (8). pp. 676-681.

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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 Angstrom 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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Nano-diffraction of Biological Specimen (Abrahams)
UniBasel Contributors:Abrahams, Jan Pieter
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Nature Publishing Co
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:21 Aug 2020 14:11
Deposited On:21 Aug 2020 14:11

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