Fig. 3: The conformation change of the connector induced by HB3089 binding. | Cell Discovery

Fig. 3: The conformation change of the connector induced by HB3089 binding.

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

Fig. 3

Side (a) and top (b) views of the connector from HB3089-bound STING, showing the two monomers of the connector and the LBDα1 form the right-handed crossover. For clarify, the cLoop2 of the connector is not shown. The map and the model are displayed in transparent surface and ribbon, respectively, and are colored as in Fig. 2b. c, d Structural comparison of the connectors between the HB3089-bound STING (red and purple) and the apo STING (grey), showing the helices and the loops of the connector from the HB3089-bound STING revolved (curved arrows) and moved downwards (arrows), respectively. The residues of Val147 are indicated by side chain showing. e, f The atomic models of the connector helices from the HB3089-bound STING (e, red and purple) and the apo STING (f, grey), showing the inter-Cα distance between residues Val147 at the connectors.

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