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Roussel, A; Mathieu, M; Dobbs, A; Luu, B; Cambillau, C; Kellenberger, C

Complexation of two proteic insect inhibitors to the active site of chymotrypsin suggests decoupled roles for binding and selectivity

Journal of Biological Chemistry 276 (42) 38893-38898

by Administrateur - published on


The crystal structures of two homologous inhibitors (PMP-C and PMP-D2v) from the insect Locusta migratoria have been determined in complex with bovine a -chymotrypsin at 2.1- and 3.0-Angstrom resolution, respectively. PMP-C is a potent bovine a -chymotrypsin inhibitor whereas native PMP-D2 is a weak inhibitor of bovine trypsin. One unique mutation at the P1 position converts PMP-D2 into a potent bovine a -chymotrypsin inhibitor.