C型凝集素
凝集素
无花果素
功能多样性
川地69
化学
生物化学
类型(生物学)
生物
计算生物学
甘露聚糖结合凝集素
生态学
细胞毒性T细胞
白细胞介素2受体
体外
标识
DOI:10.1016/s0959-440x(99)00009-3
摘要
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.
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