ArticleActa crystallographica. Section F, Structural biology communications2025
LOPAC library screening identifies suramin as a TRIM21 binder with a unique binding mode revealed by crystal structure.
Article in Acta crystallographica. Section F, Structural biology communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Redirecting TRIM21 with TRIMTACs for the targeted degradation of multimeric proteins.The FEBS journal · 2026Review
- Suramin Interactions Across Biological Systems: From Molecular Targets to Therapeutic Implications.Biomolecules · 2026Review
- Structural analysis of TRIM family PRYSPRY domains and its implications for E3-ligand design.Journal of structural biology: X · 2025Article
- Crystallographic fragment screening reveals ligand hotspots in TRIM21 PRY-SPRY domain.Communications chemistry · 2025Article
Corrections and comments
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Authors and funding
3 authors.
Funding
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).
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