5HZV
Crystal structure of the zona pellucida module of human endoglin/CD105
Summary for 5HZV
| Entry DOI | 10.2210/pdb5hzv/pdb |
| Related | 3D4G 3NK4 4WRN 5HZW 5I04 5I05 |
| Related PRD ID | PRD_900001 |
| Descriptor | Maltose-binding periplasmic protein,Endoglin, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | zona pellucida domain, angiogenesis, glycoprotein, receptor, signaling protein |
| Biological source | Escherichia coli (strain K12) More |
| Total number of polymer chains | 1 |
| Total formula weight | 68662.79 |
| Authors | Bokhove, M.,Saito, T.,Jovine, L. (deposition date: 2016-02-03, release date: 2017-06-07, Last modification date: 2024-10-23) |
| Primary citation | Saito, T.,Bokhove, M.,Croci, R.,Zamora-Caballero, S.,Han, L.,Letarte, M.,de Sanctis, D.,Jovine, L. Structural Basis of the Human Endoglin-BMP9 Interaction: Insights into BMP Signaling and HHT1. Cell Rep, 19:1917-1928, 2017 Cited by PubMed Abstract: 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. PubMed: 28564608DOI: 10.1016/j.celrep.2017.05.011 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
Download full validation report
