9KPL
Crystal structure of T. rubripes Mincle with glucose
Summary for 9KPL
| Entry DOI | 10.2210/pdb9kpl/pdb |
| Descriptor | C-type lectin domain-containing protein, alpha-D-glucopyranose, beta-D-glucopyranose, ... (5 entities in total) |
| Functional Keywords | c-type lectin, ectodomain, carbohydrate recognition doamin, immune system |
| Biological source | Takifugu rubripes (torafugu) |
| Total number of polymer chains | 2 |
| Total formula weight | 35705.75 |
| Authors | |
| Primary citation | Ito, T.,Guenther, C.,Ishikawa, E.,Yabuki, T.,Nagae, M.,Nakatani, Y.,Yamasaki, S. Phylogenetic and structural insights into the origin of C-type lectin Mincle in vertebrates. Immunogenetics, 77:18-18, 2025 Cited by PubMed Abstract: Our bodies are continuously exposed to injurious insults by infection and tissue damage, which are primarily sensed by innate immune receptors to maintain homeostasis. Among such receptors is macrophage-inducible C-type lectin (Mincle, gene symbol CLEC4E), a member of the C-type lectin receptor (CLR) family, which functions as an immune sensor for both pathogens and damaged self. To monitor these injurious stimuli, Mincle recognizes disaccharide-based pathogen-derived glycolipids and monosaccharide-based intracellular metabolites, such as β-glucosylceramide. Mincle is well-conserved among mammals; however, there are questions that remain unclear, such as from which lower vertebrate did it arise and whether the original ligand was self or non-self. Here, we found homologues of Mincle and its signaling subunit Fc receptor γ chain (FcRγ) in lower vertebrates, such as reptiles, amphibians, and fishes. The crystal structure of a Mincle homologue revealed that fish Mincle possesses a narrower sugar-binding pocket than that of mammalian Mincle, and accommodates only monosaccharide moieties. These results suggest that Mincle may have evolved from a self-recognizing receptor, and its sugar-binding pocket widened during evolution, presumably to adapt to disaccharide-based glycolipids derived from life-threatening pathogens. PubMed: 40119899DOI: 10.1007/s00251-025-01375-x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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