P. Perani et al., Mutations on the hinge region of leukocyte elastase inhibitor determine the loss of inhibitory function, BIOC BIOP R, 274(3), 2000, pp. 841-844
Citations number
19
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Leukocyte elastase inhibitor (LEI) is a cytosolic component of lung macroph
ages and blood leukocytes that inhibits neutrophil elastase. LEI is a membe
r of the serpin superfamily, these proteins, mostly protease inhibitors, ar
e thought to undergo a conformational change upon complex formation with pr
oteinase that involves partial insertion of the hinge region of the reactiv
e centre loop into a beta-sheet of the inhibitor. In this work three mutati
ons were produced in the hinge region of elastase inhibitor that abolish th
e inhibition activity of LEI and transform the protein in a substrate of th
e elastase. This result demonstrates that the inhibitory mechanism of serpi
n is common to LEI. (C) 2000 Academic Press.