9GTE
Crystal structure of TRIM21 PRY-SPRY domain bound to Suramin
Summary for 9GTE
| Entry DOI | 10.2210/pdb9gte/pdb |
| Descriptor | E3 ubiquitin-protein ligase TRIM21, 1,2-ETHANEDIOL, 8,8'-[CARBONYLBIS[IMINO-3,1-PHENYLENECARBONYLIMINO(4-METHYL-3,1-PHENYLENE)CARBONYLIMINO]]BIS-1,3,5-NAPHTHALENETRISULFON IC ACID, ... (4 entities in total) |
| Functional Keywords | trim21, pry-spry domain, suramin, e3 ligase, ligase |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 23266.05 |
| Authors | Kim, Y.,Knapp, S.,Kraemer, A.,Structural Genomics Consortium (SGC) (deposition date: 2024-09-17, release date: 2024-10-30, Last modification date: 2025-05-14) |
| Primary citation | Kim, Y.,Knapp, S.,Kramer, A. LOPAC library screening identifies suramin as a TRIM21 binder with a unique binding mode revealed by crystal structure. Acta Crystallogr.,Sect.F, 81:101-107, 2025 Cited by PubMed Abstract: Differential scanning fluorimetry screening of the Library of Pharmacologically Active Compounds (LOPAC) identified four hits for the PRYSPRY domain of the human E3 ligase tripartite motif-containing protein 21 (TRIM21). Isothermal titration calorimetry subsequently confirmed suramin as a binder with micromolar affinity. To further investigate the binding mechanism, mouse TRIM21 was used as a structural surrogate due to its improved protein stability and high sequence similarity to the human counterpart. A crystal structure of the complex refined at 1.3 Å resolution revealed a unique binding mode, providing new avenues for targeting TRIM21 and for the development of proteolysis-targeting chimeras (PROTACs). PubMed: 39955622DOI: 10.1107/S2053230X25000913 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.3 Å) |
Structure validation
Download full validation report
