8P8S
Recombinant Ym2 crystal structure
Summary for 8P8S
| Entry DOI | 10.2210/pdb8p8s/pdb |
| Descriptor | Chitinase-like protein 4, 1,2-ETHANEDIOL (3 entities in total) |
| Functional Keywords | ym2, chil4, in vivo crystallization, chitinase-like protein, immune system |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 47785.51 |
| Authors | Verschueren, K.H.G.,Verstraete, K.,Heyndrickx, I.,Smole, U.,Aegerter, A.,Savvides, S.N.,Lambrecht, B.N. (deposition date: 2023-06-02, release date: 2024-01-17, Last modification date: 2024-10-23) |
| Primary citation | Heyndrickx, I.,Deswarte, K.,Verstraete, K.,Verschueren, K.H.G.,Smole, U.,Aegerter, H.,Dansercoer, A.,Hammad, H.,Savvides, S.N.,Lambrecht, B.N. Ym1 protein crystals promote type 2 immunity. Elife, 12:-, 2024 Cited by PubMed Abstract: Spontaneous protein crystallization is a rare event, yet protein crystals are frequently found in eosinophil-rich inflammation. In humans, Charcot-Leyden crystals (CLCs) are made from galectin-10 (Gal10) protein, an abundant protein in eosinophils. Although mice do not encode Gal10 in their genome, they do form pseudo-CLCs, made from the chitinase-like proteins Ym1 and/or Ym2, encoded by and and made by myeloid and epithelial cells respectively. Here, we investigated the biological effects of pseudo-CLCs since their function is currently unknown. We produced recombinant Ym1 crystals which were shown to have identical crystal packing and structure by X-ray crystallography as in vivo native crystals derived from murine lung. When administered to the airways of mice, crystalline but not soluble Ym1 stimulated innate and adaptive immunity and acted as a type 2 immune adjuvant for eosinophilic inflammation via triggering of dendritic cells (DCs). Murine Ym1 protein crystals found at sites of eosinophilic inflammation reinforce type 2 immunity and could serve as a surrogate model for studying the biology of human CLCs. PubMed: 38194250DOI: 10.7554/eLife.90676 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.17 Å) |
Structure validation
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