The structure of a serpin–protease complex revealed by intramolecular distance measurements using donor–donor energy migration and mapping of interaction sites
- 30 April 2000
- Vol. 8 (4) , 397-405
- https://doi.org/10.1016/s0969-2126(00)00121-0
Abstract
No abstract availableKeywords
This publication has 30 references indexed in Scilit:
- Formation of the covalent serpin-proteinase complex involves translocation of the proteinase by more than 70 Å and full insertion of the reactive center loop into β-sheet AProceedings of the National Academy of Sciences, 1999
- Wild-type α1-antitrypsin is in the canonical inhibitory conformationJournal of Molecular Biology, 1998
- Structural insights into serpin—protease complexes reveal the inhibitory mechanism of serpinsNature Structural & Molecular Biology, 1997
- Rational Design of Complex Formation between Plasminogen Activator Inhibitor-1 and Its Target ProteinasesJournal of Structural Biology, 1997
- Modeling of serpin-protease complexes: Antithrombin-thrombin, α1-antitrypsin (358Met→Arg)-thrombin, α1-antitrypsin (358Met→Arg)-trypsin, and antitrypsin-elastaseProteins-Structure Function and Bioinformatics, 1996
- Structural basis for serpin inhibitor activityProteins-Structure Function and Bioinformatics, 1995
- Serpins: Mobile conformations in a family of proteinase inhibitorsCurrent Opinion in Structural Biology, 1992
- Natural protein proteinase inhibitors and their interaction with proteinasesEuropean Journal of Biochemistry, 1992
- Structural basis of latency in plasminogen activator inhibitor-1Nature, 1992
- Implications of the three-dimensional structure of .alpha.1-antitrypsin for structure and function of serpinsBiochemistry, 1989