The F-helix of serpins plays an essential, active role in the proteinase inhibition mechanism
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Reference24 articles.
1. On the size of the active site in proteases. I. Papain
2. Formation of the covalent serpin-proteinase complex involves translocation of the proteinase by more than 70 A and full insertion of the reactive center loop into -sheet A
3. The structure of a serpin–protease complex revealed by intramolecular distance measurements using donor–donor energy migration and mapping of interaction sites
4. Structure of a serpin–protease complex shows inhibition by deformation
5. Insight into the Mechanism of Serpin−Proteinase Inhibition from 2D [1H-15N] NMR Studies of the 69 kDa α1-Proteinase Inhibitor Pittsburgh−Trypsin Covalent Complex
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