9UAL
Crystal structure of Trimucrin
Summary for 9UAL
| Entry DOI | 10.2210/pdb9ual/pdb |
| Descriptor | Zinc metalloproteinase/disintegrin PMMP-2, ZINC ION, ACETATE ION, ... (4 entities in total) |
| Functional Keywords | disintegrin, platelet aggregation inhibitor, blood clotting |
| Biological source | Protobothrops mucrosquamatus |
| Total number of polymer chains | 2 |
| Total formula weight | 16463.39 |
| Authors | Chang, Y.T.,Chuang, W.J. (deposition date: 2025-04-01, release date: 2026-04-08, Last modification date: 2026-05-20) |
| Primary citation | Wang, Y.T.,Chang, Y.T.,Huang, C.H.,Liau, C.T.,Chen, C.Y.,Chuang, W.J. Structural basis for the differential recognition of integrin alpha v beta 3 by rhodostomin and trimucrin. Commun Biol, 9:-, 2026 Cited by PubMed Abstract: Rhodostomin (Rho) and Trimucrin (Tmu) are RGD-containing disintegrins that inhibit integrins more effectively than short RGD peptides. They differ in their linker, RGD loop, and C-terminal sequences. We determined the X-ray structure of Tmu and the cryo-EM structures of integrin αvβ3 in complex with both disintegrins. Structural analysis revealed subtle differences in binding, with both adopting a rigid backbone conformation and interacting with integrin through three cooperative binding sites. Besides the conserved RGD interface, Tmu features a cluster of basic residues in its linker, while Rho has distinct C-terminal interactions. Disintegrin binding stabilizes αvβ3 in an extended-open conformation, while the β3-Y110 residue is essential for maintaining the bent state without ligands. These findings enhance our understanding of integrin recognition and inform the development of integrin-targeted therapeutics for anti-angiogenic, anti-tumor, and anti-inflammatory applications. PubMed: 42045602DOI: 10.1038/s42003-026-10139-6 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.68 Å) |
Structure validation
Download full validation report
