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Mer, G ; Hietter, H ; Kellenberger, C ; Renatus, M ; Luu, B ; Lefevre, JF

Solution structure of PMP-C : A new fold in the group of small serine proteinase inhibitors

Journal of Molecular Biology 258 (1) 158-171

par Administrateur - publié le

Abstract :

The solution structure and the disulfide pairings of a 36-residue proteinase inhibitor isolated from the insect Locusta migratoria have been determined using NMR spectroscopy and simulated annealing calculations. The peptide, termed PMP-C, was previously shown to inhibit bovine cc-chymotrypsin as well as human leukocyte elastase, and was also found to block high-voltage-activated Ca2+ currents in rat sensory neurones. PMP-C has a prolate ellipsoid shape and adopts a tertiary fold hitherto unobserved in the large group of small ’’canonical’’ proteinase inhibitors.