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Modélisation moléculaire des lectines et des glycosyltransférases

Abstract : Glycosyltransferases and lectins are two protein families participating in the biosynthesis and specific recognition of glyacans. One part of this work has been dedicated to the update of database of crystallographic structures of glycosyltransferases. Homology modeling of some biologically interesting glycosyltransferases whose crystallographic structures have not been solved yet has been performed. Molecular dynamics simulations of the glycosyltransferase LgtC, which participates on the biosynthesis of lipooligosaccharides (LOS) in the bacteria Neisseria meningitidis, allowed us to propose a reaction mechanism.
PA-IIL lectin, from Pseudomoans aeruginosa, displays an unusually high affinity for fucose. Quantum chemical calculations on the model including the binding site of the lectin in complex with fucose have shown that the strong binding between the protein and the ligand could be partly due to a significant delocalization of electrostatic charges.
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https://tel.archives-ouvertes.fr/tel-00186487
Contributor : Snajdrova Lenka <>
Submitted on : Friday, November 9, 2007 - 12:03:35 PM
Last modification on : Friday, November 6, 2020 - 3:45:34 AM
Long-term archiving on: : Friday, November 25, 2016 - 5:10:57 PM

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  • HAL Id : tel-00186487, version 1

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Lenka Snajdrova. Modélisation moléculaire des lectines et des glycosyltransférases. Biologie cellulaire. Université Joseph-Fourier - Grenoble I, 2006. Français. ⟨tel-00186487⟩

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