8W9J
Crystal structure of human CLEC12A ectodomain complexed with 50C1 Fab
Summary for 8W9J
| Entry DOI | 10.2210/pdb8w9j/pdb |
| Descriptor | Anti-human CLEC12A antibody 50C1 light chain, Anti-human CLEC12A antibody 50C1 heavy chain, C-type lectin domain family 12 member A (3 entities in total) |
| Functional Keywords | c-type lectin receptor, inhibitory antibody, clec12a, immune system |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 6 |
| Total formula weight | 143004.07 |
| Authors | Mori, S.,Nagae, M.,Yamasaki, S. (deposition date: 2023-09-05, release date: 2024-03-06, Last modification date: 2024-11-13) |
| Primary citation | Mori, S.,Nagae, M.,Yamasaki, S. Crystal structure of the complex of CLEC12A and an antibody that interferes with binding of diverse ligands. Int.Immunol., 36:279-290, 2024 Cited by PubMed Abstract: C-type lectin receptors (CLRs) are a family of pattern recognition receptors, which detect a broad spectrum of ligands via small carbohydrate-recognition domains (CRDs). CLEC12A is an inhibitory CLR that recognizes crystalline structures such as monosodium urate crystals. CLEC12A also recognizes mycolic acid, a major component of mycobacterial cell walls, and suppresses host immune responses. Although CLEC12A could be a therapeutic target for mycobacterial infection, structural information on CLEC12A was not available. We report here the crystal structures of human CLEC12A (hCLEC12A) in ligand-free form and in complex with 50C1, its inhibitory antibody. 50C1 recognizes human-specific residues on the top face of hCLEC12A CRD. A comprehensive alanine scan demonstrated that the ligand-binding sites of mycolic acid and monosodium urate crystals may overlap with each other, suggesting that CLEC12A utilizes a common interface to recognize different types of ligands. Our results provide atomic insights into the blocking and ligand-recognition mechanisms of CLEC12A and leads to the design of CLR-specific inhibitors. PubMed: 38386511DOI: 10.1093/intimm/dxae006 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.5 Å) |
Structure validation
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