The Mannose-specific bulb lectin from Galanthus nivalis (snowdrop) binds mono- and dimannosides at distinct sites. Structure analysis of refined complexes at 2.3 angstrom and 3.0 angstrom resolution

The Mannose-specific bulb lectin from Galanthus nivalis (snowdrop) binds mono- and dimannosides at distinct sites. Structure analysis of refined complexes at 2.3 angstrom and 3.0 angstrom resolution
复制标题

DOI:
10.1006/jmbi.1996.0532
复制
发表时间:
1996-10-04
影响因子:
5.6
通讯作者:
Wright, CS
Wright, CS
中科院分区:
生物学2区
文献类型:
--
作者:
Hester, G;Wright, CS

文献摘要

被引文献

相似文献

雪花莲凝集素(Galanthusnivalis agglutinin,GNA)是石蒜科植物鳞茎凝集素家族的一种甘露糖特异性凝集素。已经确定了与甲基-α-D-甘露糖(MeMan)和甘露糖-α 1,3-D-甘露糖-α-OMe(MeMan-2)复合的GNA的晶体结构,并在内部结构对称性和糖结合方面进行了分析。用0.167的X因子(所有数据)精制的2.29埃正交甲基-α-Man复合物的最终模型包括12个结合的糖配体和327个水分子。222四聚体的四个独立的亚基(A、B、C和D)和构成每个亚基的三个四链β-片层(I、II和III)比较接近(r.m.s.
Galanthus nivalis agglutinin (GNA, a 50 kDa tetramer) is a mannose-specific lectin of the Amaryllidaceae family of bulb lectins. Crystal structures of GNA complexed with methyl-alpha-D-mannose (MeMan) and mannose-alpha 1,3-D-mannose-alpha-OMe (MeMan-2) have been determined and analyzed in terms of internal structural symmetry and saccharide binding. The final model of the 2.29 Angstrom orthorhombic methyl-alpha-Man complex refined with an X-factor of 0.167 (all data) includes 12 bound sugar ligands and 327 water molecules. The four independent subunits (A, B, C and D) of the 222 tetramer and the three four-stranded beta-sheets (I,II and III) that constitute each subunit compare closely (r.m.s.Delta =