TY - JOUR
T1 - Serpins and other covalent protease inhibitors
AU - Ye, Sheng
AU - Goldsmith, Elizabeth J.
N1 - Funding Information:
This research was supported by The Welch Foundation Grant.
PY - 2001/12/1
Y1 - 2001/12/1
N2 - 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.
AB - 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.
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U2 - 10.1016/S0959-440X(01)00275-5
DO - 10.1016/S0959-440X(01)00275-5
M3 - Review article
C2 - 11751056
AN - SCOPUS:0035692792
SN - 0959-440X
VL - 11
SP - 740
EP - 745
JO - Current Opinion in Structural Biology
JF - Current Opinion in Structural Biology
IS - 6
ER -