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LOPAC library screening identifies suramin as a TRIM21 binder with a unique binding mode revealed by crystal
Yeojin Kim1, Stefan Knapp1, Andreas Krämer1
1Department of Pharmacy, Goethe University Frankfurt, Max-von-Laue Strasse 9, Frankfurt am Main, 60438 Hessen, Germany.
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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