Drickamer K
Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.
Curr Opin Struct Biol. 1999 Oct;9(5):585-90. doi: 10.1016/s0959-440x(99)00009-3.
Carbohydrate-recognition domains of C-type (Ca2+-dependent) animal lectins serve as prototypes for an important family of protein modules. Only some domains in this family bind Ca2+ or sugars. A comparison of recent structures of C-type lectin-like domains reveals diversity in the modular fold, particularly in the region associated with Ca2+ and sugar binding. Some of this diversity reflects the changes that occur during normal physiological functioning of the domains. C-type lectin-like domains associate with each other through several different surfaces to form dimers and trimers, from which ligand-binding sites project in a variety of different orientations.
C型（钙离子依赖型）动物凝集素的碳水化合物识别结构域是重要蛋白质模块家族的原型。该家族中只有一些结构域能结合钙离子或糖类。对C型凝集素样结构域的最新结构进行比较后发现，模块化折叠存在多样性，尤其是在与钙离子和糖类结合相关的区域。这种多样性部分反映了这些结构域在正常生理功能过程中发生的变化。C型凝集素样结构域通过几个不同的表面相互结合形成二聚体和三聚体，配体结合位点从这些二聚体和三聚体以各种不同的方向伸出。
