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Etude des interactions entre les facteurs cytosoliques du complexe de la NADPH Oxydase

Sylvie Chenavas 1
1 LPM - Laboratoire des Protéines Membranaires
IBS - UMR 5075 - Institut de biologie structurale
Abstract : During phagocytose of a micro-organism, the NADPH Oxidase complex of neutrophiles is activated. Reactive oxygen species are then produced and contribute to pathogen destruction. This complex comprises cytosolic factors (p67phox, p40phox, p47phox), a small G protein Rac and a flavocytochrome b558 composed of p22phox and gp91phox. Mutations within the genes encoding some of these proteins lead to a rare but serious disease termed chronic granulomatous disease (CGD). The formation of the ternary complex constituted by the cytosolic factors implies several SH3 domain/polyproline interactions and also an interaction PB1 domain interaction. We structurally characterized by Nuclear Magnetic Resonance the interaction between PB1 domains of p67phox and p40phox. We also studied the consequences of activation on the interactions involving p47phox C-terminal polyproline motif and its SH3 domain partners. Thus, we combined the analysis of the structures of p40phox SH3 domain and p67phox C-terminal SH3 domain, in complex with p47phox C-terminal polyproline, with our affinity measures between these partners at various stages of activation. These data were obtained by intrinsic fluorescence of tryptophan present within SH3 domains.
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Sylvie Chenavas. Etude des interactions entre les facteurs cytosoliques du complexe de la NADPH Oxydase. Biochimie [q-bio.BM]. Université Joseph-Fourier - Grenoble I, 2005. Français. ⟨tel-00540636⟩

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