Wright L M, Reynolds C D, Rizkallah P J, Allen A K, Van Damme E J, Donovan M J, Peumans W J
School of Biomolecular Sciences, Max Perutz Building, Liverpool John Moores University, Liverpool, UK.
FEBS Lett. 2000 Feb 18;468(1):19-22. doi: 10.1016/s0014-5793(00)01109-1.
The three-dimensional structure of a 244-residue, multivalent, fetuin-binding lectin, SCAfet, isolated from bluebell (Scilla campanulata) bulbs, has been solved at 3.3 A resolution by molecular replacement using the coordinates of the 119-residue, mannose-binding lectin, SCAman, also from bluebell bulbs. Unlike most monocot mannose-binding lectins, such as Galanthus nivalis agglutinin from snowdrop bulbs, which fold into a single domain, SCAfet contains two domains with approximately 55% sequence identity, joined by a linker peptide. Both domains are made up of a 12-stranded beta-prism II fold, with three putative carbohydrate-binding sites, one on each subdomain. SCAfet binds to the complex saccharides of various animal glycoproteins but not to simple sugars.
从蓝钟花（Scilla campanulata）鳞茎中分离出的一种含有244个残基的多价胎球蛋白结合凝集素SCAfet的三维结构，已通过分子置换法，以3.3埃的分辨率解析出来，所用的坐标来自同样取自蓝钟花鳞茎的含有119个残基的甘露糖结合凝集素SCAman。与大多数单子叶甘露糖结合凝集素不同，比如来自雪花莲鳞茎的雪花莲凝集素，折叠成单个结构域，SCAfet包含两个结构域，序列同一性约为55%，由一个连接肽连接。两个结构域均由一个12链β-棱柱II折叠组成，有三个推定的碳水化合物结合位点，每个亚结构域上一个。SCAfet能结合各种动物糖蛋白的复合糖类，但不能结合单糖。
