Shape-Shifting serpins
- 1 April 1994
- journal article
- Published by Springer Nature in Nature
- Vol. 368 (6471) , 570
- https://doi.org/10.1038/368570a0
Abstract
Recent structures of members of the serine proteinase inhibitor families (serpins) continue to emphasize the flexibility of the reactive loop and suggest possible 'active' conformations.Keywords
This publication has 4 references indexed in Scilit:
- Deconvoluting serpinsNature Structural & Molecular Biology, 1994
- The intact and cleaved human antithrombin III complex as a model for serpin–proteinase interactionsNature Structural & Molecular Biology, 1994
- Serpins: Mobile conformations in a family of proteinase inhibitorsCurrent Opinion in Structural Biology, 1992
- Ligand binding: proteinase-protein inhibitor interactions: Current opinion in structural biology 1991, 1:45–52Current Opinion in Structural Biology, 1991