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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Bibliographic Details
Published in:FEBS letters 2016-04, Vol.590 (8), p.1280-1288
Main Authors: Nagae, Masamichi, Ikeda, Akemi, Hanashima, Shinya, Kojima, Takumi, Matsumoto, Naoki, Yamamoto, Kazuo, Yamaguchi, Yoshiki
Format: Article
Language:English
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
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1002/1873-3468.12162