STRUCTURE OF S-LECTIN, A DEVELOPMENTALLY-REGULATED VERTEBRATE BETA-GALACTOSIDE-BINDING PROTEIN
STRUCTURE OF S-LECTIN, A DEVELOPMENTALLY-REGULATED VERTEBRATE BETA-GALACTOSIDE-BINDING PROTEIN
复制标题
DOI：
10.1073/pnas.91.4.1428
复制
发表时间：
1994-02-15
影响因子：
11.1
通讯作者：
HERZBERG, O
中科院分区：
文献类型：
--
作者：
LIAO, DI;KAPADIA, G;HERZBERG, O
14 kDa牛脾S-凝集素与二糖N-乙酰乳糖胺在1.9埃分辨率下复合的晶体结构揭示了与豆类凝集素的惊人的结构关系，尽管缺乏序列同源性。两个单体缔合形成扩展的β-夹心，每个具有豆类凝集素典型的相同的果冻卷拓扑结构，但具有显著修剪的环和不同的二聚体缔合。每个单体结合一个N-乙酰乳糖胺分子的拓扑和空间不同的网站比豆类凝集素。碳水化合物结合位点为碳水化合物结合提供了前所未有的范例，具有独特的盐桥网络。β-半乳糖的特异性来自于限制O 4原子位置的复杂相互作用。
The crystal structure of a 14 kDa bovine spleen S-lectin complexed with the disaccharide N acetyllactosamine at 1.9-Angstrom resolution reveals a surprising structural relationship to legume lectins, despite the lack of sequence homology. Two monomers associate to form an extended beta-sandwich, each with the same jelly roll topology typical of legume lectins but with dramatically trimmed loops and with different dimer association. Each monomer binds one N-acetyl lactosamine molecule in a topologically and spatially different site than that of legume lectins. The carbohydrate-binding site provides an unprecedented paradigm for carbohydrate binding, with a unique network of salt bridges. The specificity for beta-galactose arises from intricate interactions that constrain the position of the O4 atom.