亚科
聚糖
西格莱克
免疫球蛋白超家族
C型凝集素
免疫球蛋白结构域
生物
凝集素
糖基化
糖蛋白
唾液酸
受体
计算生物学
细胞生物学
遗传学
生物化学
基因
作者
Ajit Varki,Takashi Angata
出处
期刊:Glycobiology
[Oxford University Press]
日期:2005-07-13
卷期号:16 (1): 1R-27R
被引量:519
标识
DOI:10.1093/glycob/cwj008
摘要
Animal glycan-recognizing proteins can be broadly classified into two groups—lectins (which typically contain an evolutionarily conserved carbohydrate-recognition domain [CRD]) and sulfated glycosaminoglycan (SGAG)-binding proteins (which appear to have evolved by convergent evolution). Proteins other than antibodies and T-cell receptors that mediate glycan recognition via immunoglobulin (Ig)-like domains are called “I-type lectins.” The major homologous subfamily of I‐type lectins with sialic acid (Sia)-binding properties and characteristic amino-terminal structural features are called the “Siglecs” (Sia-recognizing Ig-superfamily lectins). The Siglecs can be divided into two groups: an evolutionarily conserved subgroup (Siglecs-1, -2, and -4) and a CD33/Siglec-3‐related subgroup (Siglecs-3 and -5–13 in primates), which appear to be rapidly evolving. This article provides an overview of historical and current information about the Siglecs.
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