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http://purl.uniprot.org/citations/28564608http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28564608http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28564608http://www.w3.org/2000/01/rdf-schema#comment"Endoglin (ENG)/CD105 is an essential endothelial cell co-receptor of the transforming growth factor β (TGF-β) superfamily, mutated in hereditary hemorrhagic telangiectasia type 1 (HHT1) and involved in tumor angiogenesis and preeclampsia. Here, we present crystal structures of the ectodomain of human ENG and its complex with the ligand bone morphogenetic protein 9 (BMP9). BMP9 interacts with a hydrophobic surface of the N-terminal orphan domain of ENG, which adopts a new duplicated fold generated by circular permutation. The interface involves residues mutated in HHT1 and overlaps with the epitope of tumor-suppressing anti-ENG monoclonal TRC105. The structure of the C-terminal zona pellucida module suggests how two copies of ENG embrace homodimeric BMP9, whose binding is compatible with ligand recognition by type I but not type II receptors. These findings shed light on the molecular basis of the BMP signaling cascade, with implications for future therapeutic interventions in this fundamental pathway."xsd:string
http://purl.uniprot.org/citations/28564608http://purl.org/dc/terms/identifier"doi:10.1016/j.celrep.2017.05.011"xsd:string
http://purl.uniprot.org/citations/28564608http://purl.org/dc/terms/identifier"doi:10.1016/j.celrep.2017.05.011"xsd:string
http://purl.uniprot.org/citations/28564608http://purl.uniprot.org/core/author"Saito T."xsd:string
http://purl.uniprot.org/citations/28564608http://purl.uniprot.org/core/author"Saito T."xsd:string
http://purl.uniprot.org/citations/28564608http://purl.uniprot.org/core/author"Jovine L."xsd:string
http://purl.uniprot.org/citations/28564608http://purl.uniprot.org/core/author"Jovine L."xsd:string
http://purl.uniprot.org/citations/28564608http://purl.uniprot.org/core/author"de Sanctis D."xsd:string
http://purl.uniprot.org/citations/28564608http://purl.uniprot.org/core/author"de Sanctis D."xsd:string
http://purl.uniprot.org/citations/28564608http://purl.uniprot.org/core/author"Han L."xsd:string
http://purl.uniprot.org/citations/28564608http://purl.uniprot.org/core/author"Han L."xsd:string
http://purl.uniprot.org/citations/28564608http://purl.uniprot.org/core/author"Bokhove M."xsd:string
http://purl.uniprot.org/citations/28564608http://purl.uniprot.org/core/author"Bokhove M."xsd:string
http://purl.uniprot.org/citations/28564608http://purl.uniprot.org/core/author"Letarte M."xsd:string
http://purl.uniprot.org/citations/28564608http://purl.uniprot.org/core/author"Letarte M."xsd:string
http://purl.uniprot.org/citations/28564608http://purl.uniprot.org/core/author"Croci R."xsd:string
http://purl.uniprot.org/citations/28564608http://purl.uniprot.org/core/author"Croci R."xsd:string
http://purl.uniprot.org/citations/28564608http://purl.uniprot.org/core/author"Zamora-Caballero S."xsd:string
http://purl.uniprot.org/citations/28564608http://purl.uniprot.org/core/author"Zamora-Caballero S."xsd:string
http://purl.uniprot.org/citations/28564608http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28564608http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28564608http://purl.uniprot.org/core/name"Cell Rep."xsd:string
http://purl.uniprot.org/citations/28564608http://purl.uniprot.org/core/name"Cell Rep."xsd:string