Serpins and other covalent protease inhibitors.
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.
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Department of Biochemistry, The University of Texas Southwestern Medical Center at Dallas, 5323 Harry Hines Boulevard, Dallas, Texas 75390, USA.
Goldsmith
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EJ
D053181:Caspase 8; D053453:Caspase 9; D020169:Caspases / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D015842:Serine Proteinase Inhibitors / Q000737:chemistry*; D015843:Serpins / Q000737:chemistry*; D014357:Trypsin; D014361:Trypsin Inhibitors / Q000737:chemistry; D014764:Viral Proteins / Q000737:chemistry / Q000378:metabolism
D015842:Serine Proteinase Inhibitors; D015843:Serpins; D014361:Trypsin Inhibitors; D014764:Viral Proteins; C081618:p35 protein, Nucleopolyhedrovirus; D014357:Trypsin; D053181:Caspase 8; D053453:Caspase 9; D020169:Caspases