Loris R, Maes D, Poortmans F, Wyns L, Bouckaert J
Laboratorium voor Ultrastruktuur, Vlaams Interuniversitair Instituut voor Biotechnologie, Vrije Universiteit Brussel, Paardenstraat 65, B-1640 Sint-Genesius-Rode, Belgium.
J Biol Chem. 1996 Nov 29;271(48):30614-8. doi: 10.1074/jbc.271.48.30614.
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 alpha1-->3 linkage has a different conformation, resulting in a different part of the alpha1-->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.
伴刀豆球蛋白A与三甘露糖苷甲基-3,6-二-O-(α-D-甘露吡喃糖基)-α-D-甘露吡喃糖苷复合物的结构已在一个新的空间群中确定。在伴刀豆球蛋白A四聚体的四个亚基中的三个中，蛋白质与结合糖类之间的相互作用与其他作者先前报道的基本相同（奈史密斯，J. H.，和菲尔德，R. A.（1996年）《生物化学杂志》271，972 - 976）。然而，在第四个亚基中，α1→3连接具有不同的构象，导致α1→3连接的甘露糖的不同部分与蛋白质基本相同的表面相互作用。此外，与无糖类结构和其他碳水化合物复合物相比，在亚基的四级缔合中观察到显著差异，这表明伴刀豆球蛋白A四聚体是一个相当灵活的实体。
