5B1W
Crystal structure of human dendritic cell inhibitory receptor (DCIR) C-type lectin domain in ligand-free form
Summary for 5B1W
Entry DOI | 10.2210/pdb5b1w/pdb |
Related | 5B1X |
Descriptor | C-type lectin domain family 4 member A, CALCIUM ION (3 entities in total) |
Functional Keywords | c-type lectin domain, innate immunity, carbohydrate recognition, carbohydrate binding protein |
Biological source | Homo sapiens (Human) |
Total number of polymer chains | 4 |
Total formula weight | 63570.54 |
Authors | Nagae, M.,Yamaguchi, Y. (deposition date: 2015-12-21, release date: 2016-05-11, Last modification date: 2023-11-08) |
Primary citation | Nagae, 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: 27015765DOI: 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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