6GKT
X-ray structure of a non-autocrystallizing galectin-10 variant, Gal10-Tyr69Glu
Summary for 6GKT
| Entry DOI | 10.2210/pdb6gkt/pdb |
| Related | 6GKQ 6GKS |
| Descriptor | Galectin-10, TRIETHYLENE GLYCOL, TETRAETHYLENE GLYCOL, ... (5 entities in total) |
| Functional Keywords | non-autocrystallizing, mutant, galectin-10, sugar binding protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 6 |
| Total formula weight | 101475.77 |
| Authors | Verstraete, K.,Verschueren, K.,Savvides, S.N. (deposition date: 2018-05-21, release date: 2019-06-05, Last modification date: 2024-01-17) |
| Primary citation | Persson, E.K.,Verstraete, K.,Heyndrickx, I.,Gevaert, E.,Aegerter, H.,Percier, J.M.,Deswarte, K.,Verschueren, K.H.G.,Dansercoer, A.,Gras, D.,Chanez, P.,Bachert, C.,Goncalves, A.,Van Gorp, H.,De Haard, H.,Blanchetot, C.,Saunders, M.,Hammad, H.,Savvides, S.N.,Lambrecht, B.N. Protein crystallization promotes type 2 immunity and is reversible by antibody treatment. Science, 364:-, 2019 Cited by PubMed Abstract: Although spontaneous protein crystallization is a rare event in vivo, Charcot-Leyden crystals (CLCs) consisting of galectin-10 (Gal10) protein are frequently observed in eosinophilic diseases, such as asthma. We found that CLCs derived from patients showed crystal packing and Gal10 structure identical to those of Gal10 crystals grown in vitro. When administered to the airways, crystalline Gal10 stimulated innate and adaptive immunity and acted as a type 2 adjuvant. By contrast, a soluble Gal10 mutein was inert. Antibodies directed against key epitopes of the CLC crystallization interface dissolved preexisting CLCs in patient-derived mucus within hours and reversed crystal-driven inflammation, goblet-cell metaplasia, immunoglobulin E (IgE) synthesis, and bronchial hyperreactivity (BHR) in a humanized mouse model of asthma. Thus, protein crystals may promote hallmark features of asthma and are targetable by crystal-dissolving antibodies. PubMed: 31123109DOI: 10.1126/science.aaw4295 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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