9GTE

Crystal structure of TRIM21 PRY-SPRY domain bound to Suramin

9GTE の概要

• エントリーDOI: 10.2210/pdb9gte/pdb
• 分子名称: 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)
• 機能のキーワード: trim21, pry-spry domain, suramin, e3 ligase, ligase
• 由来する生物種: Mus musculus (house mouse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23266.05

構造登録者

Kim, Y.,Knapp, S.,Kraemer, A.,Structural Genomics Consortium (SGC) (登録日: 2024-09-17, 公開日: 2024-10-30, 最終更新日: 2025-05-14)

主引用文献

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

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: 39955622
DOI: 10.1107/S2053230X25000913

実験手法

X-RAY DIFFRACTION (1.3 Å)