Bovine heart galectin-1 selects a unique (Syn) conformation of C-lactose, a flexible lactose analogue

被引:87
作者
Asensio, JL
Espinosa, JF
Dietrich, H
Cañada, FJ
Schmidt, RR
Martín-Lomas, M
André, S
Gabius, HJ
Jiménez-Barbero, J
机构
[1] CSIC, Inst Quim Organ, Dept Quim Organ Biol, E-28006 Madrid, Spain
[2] Univ Munich, Tierarztl Fak, Inst Physiol Chem, D-80539 Munich, Germany
[3] Univ Konstanz, Inst Organ Chem, D-78464 Constance, Germany
[4] CSIC, Inst Invest Quim, E-41080 Seville, Spain
关键词
D O I
10.1021/ja990601u
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
The C-glycoside analogue of lactose harbors a pronounced flexibility in water with three conformers in equilibrium. The bound conformation of C-lactose to bovine heart galectin-1 in solution has been determined by NMR spectroscopy. It is demonstrated that the lectin selects the syn conformation of the structural analogue of natural lactose and not the global minimum, anti conformation. The bound conformer resembles those found in the crystal structures of complexes of galectin-1/N-acetyllactosamine-containing oligosaccharides and in solution for an avian galectin. Docking of the analogue within the galectin's binding site furnishes explanations, in structural terms, for the exclusive recognition of the syn conformer.
引用
收藏
页码:8995 / 9000
页数:6
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