A structure of the complex between concanavalin A and methyl-3,6-di-O-(alpha-D-mannopyranosyl)-alpha-D-mannopyranoside reveals two binding modes

被引:64
作者
Loris, R
Maes, D
Poortmans, F
Wyns, L
Bouckaert, J
机构
[1] FREE UNIV BRUSSELS VIB, LAB ULTRASTRUKTUUR, B-1640 RHODE ST GENESE, BELGIUM
[2] VLAAMSE INSTELLING TECHNOL ONDERZOEK, B-2400 MOL, BELGIUM
关键词
D O I
10.1074/jbc.271.48.30614
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The structure of concanavalin A in complex with the trimannoside methyl-3,6-di-O-(alpha-D-mannopyranosyl)-alpha-D-mannopyranoside has been determined in a novel space group, In three of the four subunits of the concanavalin A tetramer, the interactions between the protein and the bound saccharide are essentially identical to those reported previously by other authors (Naismith, J, H., and Field, R, A. (1996) J, Biol, Chem, 271, 972-976), In the fourth subunit, however, the alpha 1-->3 linkage has a different conformation, resulting in a different part of the alpha 1-->3-linked mannose interacting with essentially the same surface of the protein, Furthermore, significant differences are observed in the quaternary associations of the subunits compared with the saccharide-free structures and other carbohydrate complexes, suggesting that the concanavalin A tetramer is a rather flexible entity.
引用
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页码:30614 / 30618
页数:5
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