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Crystal structure of human dendritic cell inhibitory receptor C‐type lectin domain reveals the binding mode with N‐glycan
Human dendritic cell inhibitory receptor (DCIR) is a C‐type lectin receptor expressed in classical dendritic cells and accepts several oligosaccharide ligands including N‐glycans. Here, we report the crystal structures of human DCIR C‐type lectin domains in the absence and presence of a branched N‐g...
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Published in: | FEBS letters 2016-04, Vol.590 (8), p.1280-1288 |
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container_title | FEBS letters |
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creator | Nagae, Masamichi Ikeda, Akemi Hanashima, Shinya Kojima, Takumi Matsumoto, Naoki Yamamoto, Kazuo Yamaguchi, Yoshiki |
description | Human dendritic cell inhibitory receptor (DCIR) is a C‐type lectin receptor expressed in classical dendritic cells and accepts several oligosaccharide ligands including N‐glycans. Here, we report the crystal structures of human DCIR C‐type lectin domains in the absence and presence of a branched N‐glycan unit. The domain has a typical C‐type lectin fold and two bound calcium ions. In the ligand‐bound form, the disaccharide unit (GlcNAcβ1‐2Man) acceptably fits the electron density map, indicating that it forms the main epitope. The recognition of the nonterminal N‐glycan unit explains the relatively broad specificity of this lectin. |
doi_str_mv | 10.1002/1873-3468.12162 |
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subjects | Amino Acid Sequence Animals crystal structure Crystallography, X-Ray C‐type lectin Dendritic Cells - metabolism Humans Lectins, C-Type - chemistry Ligands Mice N‐glycan Polysaccharides - chemistry Protein Binding Protein Domains Receptors, Cell Surface - chemistry Sequence Alignment |
title | Crystal structure of human dendritic cell inhibitory receptor C‐type lectin domain reveals the binding mode with N‐glycan |
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