Citation

Ye S, Goldsmith EJ. Current Opinion in Structural Biology 2001; 11(6): 740-745.

Copyright

(Copyright © 2001)

DOI

10.1016/s0959-440x(01)00275-5

PMID

11751056

Abstract

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 alpha1-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.

Language: en

Keywords

Caspase 8; Caspase 9; Caspases; Protein Conformation; Serine Proteinase Inhibitors; Serpins; Trypsin; Trypsin Inhibitors; Viral Proteins