{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["10(1)"],"submitter":["Hou J"],"pubmed_abstract":["Endothelins and their receptors, ET<sub>A</sub> and ET<sub>B</sub>, play vital roles in maintaining vascular homeostasis. Therapeutically targeting endothelin receptors, particularly through ET<sub>A</sub> antagonists, has shown efficacy in treating pulmonary arterial hypertension (PAH) and other cardiovascular- and renal-related diseases. Here we present cryo-electron microscopy structures of ET<sub>A</sub> in complex with two PAH drugs, macitentan and ambrisentan, along with zibotentan, a selective ET<sub>A</sub> antagonist, respectively. Notably, a specialized anti-ET<sub>A</sub> antibody facilitated the structural elucidation. These structures, together with the active-state structures of ET-1-bound ET<sub>A</sub> and ET<sub>B</sub>, and the agonist BQ3020-bound ET<sub>B</sub>, in comp"],"journal":["Cell discovery"],"pagination":["79"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11286772"],"repository":["biostudies-literature"],"pubmed_title":["Structural basis of antagonist selectivity in endothelin receptors."],"pmcid":["PMC11286772"],"pubmed_authors":["Yang H","Liu J","Wu L","Jiang L","Hua T","Luo Z","Liu S","Tu G","Li X","Hou J","Liu Z","Zhang Y","Zhang X","Miao C","Tan Q","Bai F"],"additional_accession":[]},"is_claimable":false,"name":"Structural basis of antagonist selectivity in endothelin receptors.","description":"Endothelins and their receptors, ET<sub>A</sub> and ET<sub>B</sub>, play vital roles in maintaining vascular homeostasis. Therapeutically targeting endothelin receptors, particularly through ET<sub>A</sub> antagonists, has shown efficacy in treating pulmonary arterial hypertension (PAH) and other cardiovascular- and renal-related diseases. Here we present cryo-electron microscopy structures of ET<sub>A</sub> in complex with two PAH drugs, macitentan and ambrisentan, along with zibotentan, a selective ET<sub>A</sub> antagonist, respectively. Notably, a specialized anti-ET<sub>A</sub> antibody facilitated the structural elucidation. These structures, together with the active-state structures of ET-1-bound ET<sub>A</sub> and ET<sub>B</sub>, and the agonist BQ3020-bound ET<sub>B</sub>, in comp","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jul","modification":"2026-06-02T09:19:39.884Z","creation":"2026-04-16T03:13:18.084Z"},"accession":"S-EPMC11286772","cross_references":{"pubmed":["39075075"],"doi":["10.1038/s41421-024-00705-9"]}}