9B9F
Zebrafish Betaglycan Orphan Domain (zfBGo) in complex with TGF-B3 and extracellular domains of TGFBRI and TGFBRII
Summary for 9B9F
| Entry DOI | 10.2210/pdb9b9f/pdb |
| Descriptor | Transforming growth factor beta-3, Transforming growth factor beta-3 triple mutant, Transforming growth factor beta receptor type-1, ... (5 entities in total) |
| Functional Keywords | complex, betaglycan, tgfbr3, tgfb, tgfbr1, tgfbr2, membrane protein |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 10 |
| Total formula weight | 170898.78 |
| Authors | |
| Primary citation | Wieteska, L.,Taylor, A.B.,Punch, E.,Coleman, J.A.,Conway, I.O.,Lin, Y.F.,Byeon, C.H.,Hinck, C.S.,Krzysiak, T.,Ishima, R.,Lopez-Casillas, F.,Cherepanov, P.,Bernard, D.J.,Hill, C.S.,Hinck, A.P. Structures of TGF-beta with betaglycan and signaling receptors reveal mechanisms of complex assembly and signaling. Nat Commun, 16:1778-1778, 2025 Cited by PubMed Abstract: Betaglycan (BG) is a transmembrane co-receptor of the transforming growth factor-β (TGF-β) family of signaling ligands. It is essential for embryonic development, tissue homeostasis and fertility in adults. It functions by enabling binding of the three TGF-β isoforms to their signaling receptors and is additionally required for inhibin A (InhA) activity. Despite its requirement for the functions of TGF-βs and InhA in vivo, structural information explaining BG ligand selectivity and its mechanism of action is lacking. Here, we determine the structure of TGF-β bound both to BG and the signaling receptors, TGFBR1 and TGFBR2. We identify key regions responsible for ligand engagement, which has revealed binding interfaces that differ from those described for the closely related co-receptor of the TGF-β family, endoglin, thus demonstrating remarkable evolutionary adaptation to enable ligand selectivity. Finally, we provide a structural explanation for the hand-off mechanism underlying TGF-β signal potentiation. PubMed: 40011426DOI: 10.1038/s41467-025-56796-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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