{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Lenza MP"],"funding":["Center for International Business Education and Research, University of Illinois at Urbana-Champaign","H2020 Marie Sklodowska-Curie Actions","European Research Council","Agencia Estatal de Investigaci?n"],"pagination":["204-215"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9875244"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["3(1)"],"pubmed_abstract":["Human sialic acid binding immunoglobulin-like lectin-8 (Siglec-8) is an inhibitory receptor that triggers eosinophil apoptosis and can inhibit mast cell degranulation when engaged by specific monoclonal antibodies (mAbs) or sialylated ligands. Thus, Siglec-8 has emerged as a critical negative regulator of inflammatory responses in diverse diseases, such as allergic airway inflammation. Herein, we have deciphered the molecular recognition features of the interaction of Siglec-8 with the mAb lirentelimab (2C4, under clinical development) and with a sialoside mimetic with the potential to suppress mast cell degranulation. The three-dimensional structure of Siglec-8 and the fragment antigen binding (Fab) portion of the anti-Siglec-8 mAb 2C4, solved by X-ray crystallography, reveal that 2C4 bin"],"journal":["JACS Au"],"pubmed_title":["Structures of the Inhibitory Receptor Siglec-8 in Complex with a High-Affinity Sialoside Analogue and a Therapeutic Antibody."],"pmcid":["PMC9875244"],"funding_grant_id":["788143","PID2019-107770RA-I00","788143-RECGLYCANMR","956758","860325"],"pubmed_authors":["Lenza MP","Quintana JI","Atxabal U","Delgado S","Ereno-Orbea J","Nunez-Franco R","Unione L","Franconetti A","Marcelo F","Schubert M","Oyenarte I","Paulson JC","Garnica Marroquin CT","Jimenez-Oses G","Nycholat C","Coelho H","Jimenez-Barbero J"],"additional_accession":[]},"is_claimable":false,"name":"Structures of the Inhibitory Receptor Siglec-8 in Complex with a High-Affinity Sialoside Analogue and a Therapeutic Antibody.","description":"Human sialic acid binding immunoglobulin-like lectin-8 (Siglec-8) is an inhibitory receptor that triggers eosinophil apoptosis and can inhibit mast cell degranulation when engaged by specific monoclonal antibodies (mAbs) or sialylated ligands. Thus, Siglec-8 has emerged as a critical negative regulator of inflammatory responses in diverse diseases, such as allergic airway inflammation. Herein, we have deciphered the molecular recognition features of the interaction of Siglec-8 with the mAb lirentelimab (2C4, under clinical development) and with a sialoside mimetic with the potential to suppress mast cell degranulation. The three-dimensional structure of Siglec-8 and the fragment antigen binding (Fab) portion of the anti-Siglec-8 mAb 2C4, solved by X-ray crystallography, reveal that 2C4 bin","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Jan","modification":"2026-07-14T19:05:32.202Z","creation":"2025-04-07T03:18:57.07Z"},"accession":"S-EPMC9875244","cross_references":{"pubmed":["36711084"],"doi":["10.1021/jacsau.2c00592"]}}