{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Akkermans O"],"funding":["Wellcome Trust","Engineering and Physical Sciences Research Council"],"pagination":["3931-3949.e26"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9596381"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["185(21)"],"pubmed_abstract":["Neural migration is a critical step during brain development that requires the interactions of cell-surface guidance receptors. Cancer cells often hijack these mechanisms to disseminate. Here, we reveal crystal structures of Uncoordinated-5 receptor D (Unc5D) in complex with morphogen receptor glypican-3 (GPC3), forming an octameric glycoprotein complex. In the complex, four Unc5D molecules pack into an antiparallel bundle, flanked by four GPC3 molecules. Central glycan-glycan interactions are formed by N-linked glycans emanating from GPC3 (N241 in human) and C-mannosylated tryptophans of the Unc5D thrombospondin-like domains. MD simulations, mass spectrometry and structure-based mutants validate the crystallographic data. Anti-GPC3 nanobodies enhance or weaken Unc5-GPC3 binding and, toget"],"journal":["Cell"],"pubmed_title":["GPC3-Unc5 receptor complex structure and role in cell migration."],"pmcid":["PMC9596381"],"funding_grant_id":["EP/S025243/1","EP/R029164/1","202827/Z/16/Z"],"pubmed_authors":["Chavent M","Zaballa S","Huo J","Del Toro D","Seiradake E","Ben Amar D","McCubbin PTN","Owens RJ","White ES","Delloye-Bourgeois C","Peregrina C","Robinson CV","Berbeira-Santana M","Comoletti D","Lowe E","Akkermans O","Pakos I","Reynaud F","Agirre J","Raj R","Aksu M","Carrasquero-Ordaz M","Kokolaki M","Castellani V"],"additional_accession":[]},"is_claimable":false,"name":"GPC3-Unc5 receptor complex structure and role in cell migration.","description":"Neural migration is a critical step during brain development that requires the interactions of cell-surface guidance receptors. Cancer cells often hijack these mechanisms to disseminate. Here, we reveal crystal structures of Uncoordinated-5 receptor D (Unc5D) in complex with morphogen receptor glypican-3 (GPC3), forming an octameric glycoprotein complex. In the complex, four Unc5D molecules pack into an antiparallel bundle, flanked by four GPC3 molecules. Central glycan-glycan interactions are formed by N-linked glycans emanating from GPC3 (N241 in human) and C-mannosylated tryptophans of the Unc5D thrombospondin-like domains. MD simulations, mass spectrometry and structure-based mutants validate the crystallographic data. Anti-GPC3 nanobodies enhance or weaken Unc5-GPC3 binding and, toget","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Oct","modification":"2026-05-03T10:34:16.076Z","creation":"2024-10-14T23:04:53.917Z"},"accession":"S-EPMC9596381","cross_references":{"pubmed":["36240740"],"doi":["10.1016/j.cell.2022.09.025"]}}