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5B1W

Crystal structure of human dendritic cell inhibitory receptor (DCIR) C-type lectin domain in ligand-free form

Summary for 5B1W
Entry DOI10.2210/pdb5b1w/pdb
Related5B1X
DescriptorC-type lectin domain family 4 member A, CALCIUM ION (3 entities in total)
Functional Keywordsc-type lectin domain, innate immunity, carbohydrate recognition, carbohydrate binding protein
Biological sourceHomo sapiens (Human)
Total number of polymer chains4
Total formula weight63570.54
Authors
Nagae, M.,Yamaguchi, Y. (deposition date: 2015-12-21, release date: 2016-05-11, Last modification date: 2023-11-08)
Primary citationNagae, M.,Ikeda, A.,Hanashima, S.,Kojima, T.,Matsumoto, N.,Yamamoto, K.,Yamaguchi, Y.
Crystal structure of human dendritic cell inhibitory receptor C-type lectin domain reveals the binding mode with N-glycan
Febs Lett., 590:1280-1288, 2016
Cited by
PubMed Abstract: 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.
PubMed: 27015765
DOI: 10.1002/1873-3468.12162
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.05 Å)
Structure validation

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