Article
Inactive conformation of the serpin alpha(1)-antichymotrypsin indicates two-stage insertion of the reactive loop: implications for inhibitory function and conformational disease.
Proceedings of the National Academy of Sciences of the United States of America - 4 Jan 2000
Gooptu B, Hazes B, Chang W S, Dafforn T R, Carrell R W, Read R J, Lomas D A
Abstract excerpt
The serpins are a family of proteinase inhibitors that play a central role in the control of proteolytic cascades. Their inhibitory mechanism depends on the intramolecular insertion of the reactive loop into beta-sheet A after cleavage by the target proteinase. Point mutations within the protein can allow aberrant conformational transitions characterized by beta-strand exchange between the reactive loop of one...
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