Oct 12, 2023 · 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...

Apr 6, 2022 · STING is a transmembrane dimeric protein that is located in the endoplasmic reticulum or in the Golgi apparatus. STING is activated by the binding of its cytoplasmic...

Mar 6, 2019 · The cytoplasmic domain of STING forms a dimer, which undergoes a conformational change upon binding to cGAMP9,14. However, it remains unclear how this conformational change leads to STING...

Jul 11, 2019 · Our insights explain the tight control of STING signaling given varying background activation signals and provide a therapeutic hypothesis for autoimmune syndrome treatment.

Our structural, functional and mutagenesis studies defined the dimer interface of STING and characterized the structure of c-di-GMP bound to the STING CTD. New insights into the understanding of c-di-GMP-mediated TBK1 signaling are provided.

Apr 21, 2023 · The STING dimer and polymer axes formed a perpendicular intersection from the top view (Figure 5B). The interactions between neighboring STING protomers not only occurred at the LBD (Figure 6A) but also existed between the TMDs (Figure 6B).

In all three ligand-bound human STING structures, we observed the closed STING dimer angle, which differs from the open dimer observed in the apo STING crystal structure (PDB: 4F5W) (Figure 1B).

Here we present cryo-electron microscopy structures of full-length STING from human and chicken in the inactive dimeric state (about 80 kDa in size), as well as cGAMP-bound chicken STING in both the dimeric and tetrameric states.

May 1, 2020 · Crystallographic and cryo-EM structures of cytosolic and full-length STING (respectively) reveal a side to side dimer packing interface of the functional STING polymer. The C-terminal tail of STING autoinhibits inactive STING and is released upon ligand binding to interact directly with downstream signaling molecules TBK1 and IRF3.

2 days ago · Full-length STING exists as an obligate dimer with an N-terminal transmembrane domain (TMD) and a C-terminal LBD separated by a connector helix 37. cGAMP binding prompts a drastic 180° rotation ...