Figure 1
From: Atomic visualization of a flipped-back conformation of bisected glycans bound to specific lectins
Multiple glycan conformations and unique selection by individual lectins.
(A) The working hypothesis of this study. A flexible glycan assumes various stable or metastable conformations (e.g. conformation A–C) and each lectin (e.g. lectin A–C) selects one specific conformation among them. (B) Representative chemical structure of a bisected biantennary complex-type N-glycan. Carbohydrate residues and each glycosidic linkage are labeled in red. (C) Chemical modification of bisecting N-acetylglucosamine (GlcNAc) catalyzed by GnT-III. Two major conformations, extend and back-fold, are shown. (D) Detection of bisected glycans in mice brain extracts by Calsepa and PHA-E lectins. Proteins were extracted from brain membrane fractions of 20-week-old wild-type or Mgat3-defiicient mice and then incubated with E4-PHA-beads. The membrane extracts (input) and proteins bound to the beads (E4-pulldown) were blotted with E4-PHA lectin or Calsepa lectin. Asterisks indicate avidin-reactive non-specific bands.
