Conformational Selection in Glycomimetics: Human Galectin-1 Only Recognizes syn-Psi-Type Conformations of beta-1,3-Linked Lactose and Its C-Glycosyl Derivative - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Chemistry - A European Journal Année : 2013

Conformational Selection in Glycomimetics: Human Galectin-1 Only Recognizes syn-Psi-Type Conformations of beta-1,3-Linked Lactose and Its C-Glycosyl Derivative

Résumé

The human lectin galectin-1 (hGal-1) translates sugar signals, that is, beta-galactosides, into effects on the level of cells, for example, growth regulation, and has become a model for studying binding of biopharmaceutically relevant derivatives. Bound-state conformations of Gal beta-C-(1 -> 3)-Glc beta-OMe (1) and its beta Gal-(1 -> 3)-beta Glc-OMe disaccharide parent compound were studied by using NMR spectroscopy (transferred (TR)-NOESY data), assisted by docking experiments and molecular dynamics (MD) simulations. The molecular recognition process involves a conformational selection event. Although free C-glycoside access four distinct conformers in solution, hGal-1 recognizes shape of a local minimum of compound 1, the syn-Phi/syn-Psi conformer, not the structure at global minimum. MD simulations were run to explain, in structural terms, the observed geometry of the complex

Dates et versions

hal-00989845 , version 1 (12-05-2014)

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P. Vidal, V. Roldos, M. Fernandez-Alonso, B. Vauzeilles, Y. Blériot, et al.. Conformational Selection in Glycomimetics: Human Galectin-1 Only Recognizes syn-Psi-Type Conformations of beta-1,3-Linked Lactose and Its C-Glycosyl Derivative. Chemistry - A European Journal, 2013, 19 (43), pp.14581-14590. ⟨10.1002/chem.201301244⟩. ⟨hal-00989845⟩
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