Circular permutation of amino acid sequences among legume lectins
Circular permutation of amino acid sequences among legume lectins
复制标题
豆类凝集素氨基酸序列的循环排列
DOI：
10.1016/0968-0004(83)90260-8
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发表时间：
1983
影响因子：
13.8
通讯作者：
B. A. Cunningham
中科院分区：
文献类型：
--
作者：
J. Hemperly;B. A. Cunningham
凝集素是存在于多种生物体中的碳水化合物结合蛋白，是一组多样化的蛋白质。然而，许多来自豆科植物的凝集素彼此密切相关，并且通过氨基酸序列的不寻常的环状排列与刀豆凝集素伴刀豆球蛋白A相关。凝集素是一类具有立体特异性和可逆结合碳水化合物的能力的蛋白质，特别是糖蛋白和糖脂的糖部分1。这些蛋白质已经在植物、细菌、细胞黏菌、无脊椎动物和脊椎动物中发现，但它们的正常生物学功能在很大程度上是未知的。脊椎动物肝脏凝集素可能是最好的特点，在其生理功能。这种分子在去唾液酸糖蛋白的摄取及其从血流中去除中起关键作用2。几乎所有的其他凝集素都与各种类型的细胞间相互作用有关。细菌凝集素被认为提供了一种微生物在感染前附着于上皮细胞和组织的手段。
Lectins, the carbohydrate-binding proteins found in a variety of organisms, are a diverse group of proteins. Many lectins from leguminous plants, however, are closely related to each other and are related to the jack bean lectin Concanavalin A by an unusual circular permutation of amino acid sequences.Lectins are an assortment of proteins that share the ability to bind stereospecifically and reversibly to carbohydrates, in particular to the sugar moieties of glycoproteins and glycolipids 1. These proteins have been found in plants, bacteria, cellular slime molds, invertebrates and vertebrates but their normal biological functions are largely unknown. The lectin from vertebrate liver is probably the most well characterized in terms of its physiological function. This molecule plays a key role in the uptake of desialyated glycoproteins and their removal from the blood stream 2. Nearly all of the other lectins have been implicated in various types of cell--cell interactions. Bacterial lectins are presumed to provide a means by which micro-organisms can attach to epithelial cells and tissues prior to infec-