Sugar recognition and protein-protein interaction of mammalian lectins conferring diverse functions

被引:28
|
作者
Nagae, Masamichi [1 ]
Yamaguchi, Yoshiki [1 ]
机构
[1] RIKEN Max Planck Joint Res Ctr, RIKEN Global Res Cluster, Syst Glycobiol Res Grp, Struct Glycobiol Team, Wako, Saitama 3510198, Japan
关键词
COMPLEX N-GLYCANS; STRUCTURAL-BASIS; PILR-ALPHA; CEL-III; SELECTIVE RECOGNITION; BACTERICIDAL LECTIN; RECEPTOR GALECTIN-8; BINDING PROTEIN; MOLECULAR-BASIS; CROSS-LINKING;
D O I
10.1016/j.sbi.2015.08.005
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Recent advances in structural analyses of mammalian lectins reveal atomic-level details of their fine specificities toward diverse endogenous and exogenous glycans. Local variations on a common scaffold can enable certain lectins to recognize complex carbohydrate ligands including branched glycans and O-glycosylated peptides. Simultaneous recognition of both glycan and the aglycon moieties enhances the affinity and specificity of lectins such as CLEC-2 and PILR alpha. Attention has been paid to the roles of galectin and RegIII family of proteins in protein-protein interactions involved in critical biological functions including signal transduction and bactericidal pore formation.
引用
收藏
页码:108 / 115
页数:8
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