2020年
Structural Aspects of Carbohydrate Recognition Mechanisms of C-Type Lectins
Current Topics in Microbiology and Immunology
- ,
- 巻
- 429
- 号
- 開始ページ
- 147
- 終了ページ
- 176
- 記述言語
- 英語
- 掲載種別
- 論文集(書籍)内論文
- DOI
- 10.1007/82_2019_181
Carbohydrate recognition is an essential function occurring in all living organisms. Lectins are carbohydrate-binding proteins and are classified into several families. In mammals, Ca -dependent C-type lectins, such as β-galactoside-binding galectin and sialic acid-binding siglec, play crucial roles in the immune response and homeostasis. C-type lectins are abundant and diverse in animals. Their immunological activities include lymphocyte homing, pathogen recognition, and clearance of apoptotic bodies. C-type lectin domains are composed of 110–130 amino acid residues with highly conserved structural folds. Remarkably, individual lectins can accept a wide variety of sugar ligands and can distinguish subtle structural differences in closely related ligands. In addition, several C-type lectin-like proteins specifically bind to carbohydrate ligands in Ca -independent ways. The accumulated 3D structural evidence clarifies the unexpected structural versatility of C-type lectins underlying the variety of ligand binding modes. In this issue, we focus on the structural aspects of carbohydrate recognition mechanisms of C-type lectins and C-type lectin-like proteins. 2+ 2+
- リンク情報
- ID情報
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- DOI : 10.1007/82_2019_181
- ISSN : 0070-217X
- eISSN : 2196-9965
- PubMed ID : 31781867
- SCOPUS ID : 85094966836