4.5 Article

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

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CURRENT OPINION IN STRUCTURAL BIOLOGY
卷 34, 期 -, 页码 108-115

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CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2015.08.005

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  1. Ministry of Education, Culture, Sports, Science, and Technology (MEXT) of Japan [26110724, 25460054]
  2. Grants-in-Aid for Scientific Research [26110724, 15K18496, 25460054] Funding Source: KAKEN

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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.

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