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- Title
Conformational Selection in Glycomimetics: Human Galectin-1 Only Recognizes syn- Ψ-Type Conformations of β-1,3-Linked Lactose and Its C-Glycosyl Derivative.
- Authors
Vidal, Paloma; Roldós, Virginia; Fernández‐Alonso, María del Carmen; Vauzeilles, Boris; Bleriot, Yves; Cañada, F. Javier; André, Sabine; Gabius, Hans‐Joachim; Jiménez‐Barbero, Jesús; Espinosa, Juan Félix; Martín‐Santamaría, Sonsoles
- Abstract
The human lectin galectin-1 (hGal-1) translates sugar signals, that is, β-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 Galβ- C-(1→3)-Glcβ- OMe ( 1) and its βGal-(1→3)-βGlc-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- Φ/ syn- Ψ conformer, not the structure at global minimum. MD simulations were run to explain, in structural terms, the observed geometry of the complex.
- Subjects
GALECTINS; GALACTOSIDES; MOLECULAR dynamics; NUCLEAR magnetic resonance spectroscopy; MOLECULAR recognition; SPECTRUM analysis; LIGAND binding (Biochemistry)
- Publication
Chemistry - A European Journal, 2013, Vol 19, Issue 43, p14581
- ISSN
0947-6539
- Publication type
Article
- DOI
10.1002/chem.201301244