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- Title
Beyond natural targets: chemical synthesis reprograms the target specificity of rapamycin.
- Authors
Zhang, Ziyang
- Abstract
As a potent (sub-nanomolar) inhibitor of the protein kinase mTOR, rapamycin exerts its pharmacological function with an unusual mechanism - it binds to the abundant cellular protein FKBP12, and the resulting binary complex engages mTOR to form an inhibitory ternary complex. Interestingly, the authors also observed FKBP12-independent binding between rapadocin and ENT1, although the interaction was much stronger with the participation of FKBP12. Rapadocin inhibited nucleoside transport by forming a ternary complex between FKBP12 and the equilibrative nucleoside transporter ENT1.
- Subjects
CHEMICAL synthesis; RAPAMYCIN; ADENOSINES; NUCLEOSIDE transport proteins; MACROCYCLIC compounds
- Publication
National Science Review, 2022, Vol 9, Issue 11, p1
- ISSN
2095-5138
- Publication type
Article
- DOI
10.1093/nsr/nwac039