期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 288, 期 47, 页码 33598-33610出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M113.513572
关键词
Carbohydrate; Crystal Structure; Dendritic Cells; Lectin; Receptors; C-type Lectin; DCIR2; Bisecting N-Acetylglucosamine; Glycan
资金
- Ministry of Education, Culture, Sports, Science, and Technology of Japan [25460054, 24770111]
- Grants-in-Aid for Scientific Research [24770111, 24770102, 25460054] Funding Source: KAKEN
Dendritic cell inhibitory receptor 2 (DCIR2) is a C-type lectin expressed on classical dendritic cells. We recently identified the unique ligand specificity of mouse DCIR2 (mDCIR2) toward biantennary complex-type glycans containing bisecting N-acetylglucosamine (GlcNAc). Here, we report the crystal structures of the mDCIR2 carbohydrate recognition domain in unliganded form as well as in complex with an agalactosylated complex-type N-glycan unit carrying a bisecting GlcNAc residue. Bisecting GlcNAc and the 1-3 branch of the biantennary oligosaccharide asymmetrically interact with canonical and non-canonical mDCIR2 residues. Ligand-protein interactions occur directly through mDCIR2-characteristic amino acid residues as well as via a calcium ion and water molecule. Our structural and biochemical data elucidate for the first time the unique binding mode of mDCIR2 for bisecting GlcNAc-containing glycans, a mode that contrasts sharply with that of other immune C-type lectin receptors such as DC-SIGN.
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