Activation of human STING by a molecular glue-like compound
- Nat Chem Biol. 2023 Oct 12. doi: 10.1038/s41589-023-01434-y.
- 1. Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX, USA.
- 2. Novartis Institutes for BioMedical Research, Cambridge, MA, USA. [email protected].
- 3. Novartis Institutes for BioMedical Research, Cambridge, MA, USA.
- 4. Novartis Institutes for BioMedical Research, San Diego, CA, USA.
- 5. Aduro Biotech, Inc., Berkeley, CA, USA.
- 6. Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX, USA. [email protected].
- 7. Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX, USA. [email protected].
- 8. Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX, USA. [email protected].
- 9. Department of Cell Biology, University of Texas Southwestern Medical Center, Dallas, TX, USA. [email protected].
- 10. Novartis Institutes for BioMedical Research, Cambridge, MA, USA. [email protected].
- # Contributed equally.
Stimulator of interferon genes (STING) is a dimeric transmembrane adapter protein that plays a key role in the human innate immune response to Infection and has been therapeutically exploited for its antitumor activity. The activation of STING requires its high-order oligomerization, which could be induced by binding of the endogenous ligand, cGAMP, to the cytosolic ligand-binding domain. Here we report the discovery through functional screens of a class of compounds, named NVS-STGs, that activate human STING. Our cryo-EM structures show that NVS-STG2 induces the high-order oligomerization of human STING by binding to a pocket between the transmembrane domains of the neighboring STING dimers, effectively acting as a molecular glue. Our functional assays showed that NVS-STG2 could elicit potent STING-mediated immune responses in cells and antitumor activities in animal models.
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Cat. No.Product NameDescriptionTargetResearch Area
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Research Areas: Cancer