Serpins and other covalent protease inhibitors

Research output: Contribution to journalReview articlepeer-review

95 Scopus citations


Serpins are irreversible covalent 'suicide' protease inhibitors. In the past two years, important advances in the structural biology of serpins have been forthcoming with the crystal structures of a covalent complex between trypsin and α1-antitrypsin, and of a Michaelis encounter complex between trypsin S195A and serpin 1B from Manduca sexta. These structures have helped elucidate many aspects of the mechanism of action of serpins. Also, the crystal structure of the cysteine protease caspase-8 in complex with the inhibitor p35 has revealed a new family of suicide protease inhibitors.

Original languageEnglish (US)
Pages (from-to)740-745
Number of pages6
JournalCurrent Opinion in Structural Biology
Issue number6
StatePublished - Dec 1 2001

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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