Relations structure/activité dans les systèmes protéiques : Chémokines et Méthionine Sulfoxyde Réductases

Abstract : We have determined by fluorescence spectroscopy the apparent dissociation constant (Kd') of the bimolecular interaction between CXCR4- and its ligand-derived synthetic peptides, which supports a simplified model for interaction of chemokine SDF-1/CXCR4 . We show also that the ERK1/2 phosphorylation is activated in a dose-dependent manner following stimulation of CHP100 cells with SDF-1-related peptides and that more than one site could assist receptor activation, and an agonist of CXCR4 it been analyzed by NMR. This study also presents the molecular functioning and structure of plant type A methionine sulfoxide reductases (MsrA). The enzyme is monomeric and active in the reduction of methionine sulfoxide with thioredoxins as a reductant. Site-directed mutagenesis indicates that three cysteines are involved in catalysis/regeneration by thioredoxin. As observed with other MsrA, in the tridimensional structure of the plastidial enzyme, the three cysteinyl residues are far apart, but the X-ray model shows for the first time a more structured C-terminal end. The conformational changes it would imply during catalysis are evaluated by molecular modelling.
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Pasquale Palladino. Relations structure/activité dans les systèmes protéiques : Chémokines et Méthionine Sulfoxyde Réductases. Autre. Université Henri Poincaré - Nancy 1, 2004. Français. ⟨NNT : 2004NAN10127⟩. ⟨tel-01748114⟩

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