3VYJ
Crystal structure of C-type lectin domain of murine dendritic cell inhibitory receptor 2 (apo form)
Summary for 3VYJ
| Entry DOI | 10.2210/pdb3vyj/pdb |
| Related | 3VYK |
| Descriptor | C-type lectin domain family 4, member a4, SULFATE ION (3 entities in total) |
| Functional Keywords | c-type lectin fold, cell surface, carbohydrate binding protein |
| Biological source | Mus musculus (mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 15248.83 |
| Authors | Nagae, M.,Yamanaka, K.,Hanashima, S.,Ikeda, A.,Satoh, T.,Matsumoto, N.,Yamamoto, K.,Yamaguchi, Y. (deposition date: 2012-09-26, release date: 2013-10-02, Last modification date: 2024-11-06) |
| Primary citation | Nagae, M.,Yamanaka, K.,Hanashima, S.,Ikeda, A.,Morita-Matsumoto, K.,Satoh, T.,Matsumoto, N.,Yamamoto, K.,Yamaguchi, Y. Recognition of Bisecting N-Acetylglucosamine: STRUCTURAL BASIS FOR ASYMMETRIC INTERACTION WITH THE MOUSE LECTIN DENDRITIC CELL INHIBITORY RECEPTOR 2 J.Biol.Chem., 288:33598-33610, 2013 Cited by PubMed Abstract: 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 α1-3 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. PubMed: 24108122DOI: 10.1074/jbc.M113.513572 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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