Fig. 2: The HB3089-induced conformational changes of ligand-binding domain of STING. | Cell Discovery

Fig. 2: The HB3089-induced conformational changes of ligand-binding domain of STING.

From: Structural insights into a shared mechanism of human STING activation by a potent agonist and an autoimmune disease-associated mutation

Fig. 2

a A side view showing the density map of the HB3089-bound STING. The two monomers and the HB3089 are colored in purple, red and yellow, respectively. b A ribbon representation of the HB3089-bound STING. The two monomers and HB3089 are colored as in a. c The atomic model of a STING monomer. The LBD, the connector, the TMD and the N-terminal loop are colored in orange, red, blue and pink, respectively. The connector links LBDα1 of the LBD to the first transmembrane helix (TM1) of the TMD through the C- and N- terminal loop of the connector (cLoop1 and cLoop2, respectively). d Structural comparison between the apo full-length STING (PDB 6NT5) and the HB3089-bound full-length STING (this study). The HB3089-bound STING is colored as that in b. The apo STING is colored in grey. e A top view of the boxed region in d, showing the conformational change of the LBD. f, g The inter-Cα distance between residues His185 at LBDα1 of the two STING forms in d.

Back to article page