Rini J M
Department of Molecular and Medical Genetics, University of Toronto, Ontario, Canada.
Annu Rev Biophys Biomol Struct. 1995;24:551-77. doi: 10.1146/annurev.bb.24.060195.003003.
Lectins comprise a structurally very diverse class of proteins characterized by their ability to bind carbohydrates with considerable specificity. They are found in organisms ranging from viruses and plants to humans and serve to mediate biological recognition events. Although lectins bind monosaccharides rather weakly, they employ common strategies for enhancing both the affinity and specificity of their interactions for more complex carbohydrate ligands. The terms subsite and subunit multivalency are defined to describe the ways in which these enhancements are achieved. Analysis of the X-ray crystal structures of different lectin types serves to illustrate how, in structural terms, subsite and subunit multivalency confer context-specific functional properties.
凝集素是一类结构极为多样的蛋白质，其特点是能够以相当高的特异性结合碳水化合物。它们存在于从病毒、植物到人类的各种生物体中，起到介导生物识别事件的作用。尽管凝集素与单糖的结合较弱，但它们采用常见策略来增强与更复杂碳水化合物配体相互作用的亲和力和特异性。亚位点和亚基多价性这两个术语被定义用于描述实现这些增强作用的方式。对不同类型凝集素的X射线晶体结构分析有助于说明，从结构角度来看，亚位点和亚基多价性是如何赋予特定环境下的功能特性的。
