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• W2070291137 abstract "Herein, we report the intrinsic conformational preferences of α-d-Manp-(1→6)-α,β-d-Manp, (1) in the free state and as two (ASAI and ConA) lectin-bound forms. NMR spectroscopy and molecular dynamics techniques are used as 3D-structural determination tools. In free form disaccharide 1 displays a fair amount of conformational freedom, with one major (ϕ/ψ 95 ± 30°/195 ± 20°) and one minor (95 ± 30°/70 ± 20°) conformations around the glycosidic linkage and around the ω angle, both the gg and gt rotamers are almost equally populated. This is a first report of a three-dimensional structure of 1 bound with ASAI. Both lectins recognize a major ϕ/ψ 95 ± 30°/200 ± 30° conformer with the ligand showing more flexibility in the binding site of ConA. Comparison of the mode of binding of the two lectins explains the differences in observed specificities." @default.
• W2070291137 created "2016-06-24" @default.
• W2070291137 creator A5003506028 @default.
• W2070291137 creator A5074261594 @default.
• W2070291137 date "2010-01-01" @default.
• W2070291137 modified "2023-09-24" @default.
• W2070291137 title "Conformational behavior of α-d-mannopyranosyl-(1→6)-α,β-d-mannose complexed with two mannose-binding plant lectins, Allium sativam agglutinin I and concanavalin A, using NMR and molecular modeling techniques" @default.
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• W2070291137 doi "https://doi.org/10.1016/j.carres.2009.09.022" @default.
• W2070291137 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19892324" @default.
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