{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ning Y"],"funding":["China Scholarship Council","Austrian Science Fund FWF","Deutsche Forschungsgemeinschaft"],"pagination":["24924-24934"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7618453"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["68(23)"],"pubmed_abstract":["C-Type lectins are a large family of carbohydrate-binding proteins. Langerin is a member of this family and is expressed by Langerhans cells, involved in pathogen recognition and innate immune activation, making it a target for small-molecule modulation in immunology and infectious diseases. We previously identified thiazolopyrimidinones as a series of allosteric inhibitors, but the underlying mechanism remained unclear. In this study, <sup>43</sup>Ca NMR demonstrated that these fragments induce Ca<sup>2+</sup> release from the receptor. Our ITC data suggested a competitive relationship between inhibitors and Ca<sup>2+</sup>, which was further validated by <sup>19</sup>F NMR spectroscopy showing inhibition of carbohydrate binding. Surprisingly, the fragment binding site was found to be loc"],"journal":["Journal of medicinal chemistry"],"pubmed_title":["Calcium Competitive Inhibition of Langerin by Thiazolopyrimidinones."],"pmcid":["PMC7618453"],"funding_grant_id":["10.55776/I5771N","I 5157","10.55776/I5157","669831-NA1274/7-1","I 5771","202106790019"],"pubmed_authors":["Turhan E","Ruwolt M","Neu U","Nazare M","Kohnke J","Rademacher C","Lefebre J","Efrem NL","Kurzbach D","Besch M","Ning Y","Amoussa M","Loll B","Zheng D"],"additional_accession":[]},"is_claimable":false,"name":"Calcium Competitive Inhibition of Langerin by Thiazolopyrimidinones.","description":"C-Type lectins are a large family of carbohydrate-binding proteins. Langerin is a member of this family and is expressed by Langerhans cells, involved in pathogen recognition and innate immune activation, making it a target for small-molecule modulation in immunology and infectious diseases. We previously identified thiazolopyrimidinones as a series of allosteric inhibitors, but the underlying mechanism remained unclear. In this study, <sup>43</sup>Ca NMR demonstrated that these fragments induce Ca<sup>2+</sup> release from the receptor. Our ITC data suggested a competitive relationship between inhibitors and Ca<sup>2+</sup>, which was further validated by <sup>19</sup>F NMR spectroscopy showing inhibition of carbohydrate binding. Surprisingly, the fragment binding site was found to be loc","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Dec","modification":"2026-06-10T05:17:48.117Z","creation":"2026-06-10T03:07:27.953Z"},"accession":"S-EPMC7618453","cross_references":{"pubmed":["41261040"],"doi":["10.1021/acs.jmedchem.5c01756"]}}