Fig. 2: Universal and unique aspects of different G protein coupling by CRF2R. | Nature Communications

Fig. 2: Universal and unique aspects of different G protein coupling by CRF2R.

From: Structure insights into selective coupling of G protein subtypes by a class B G protein-coupled receptor

Fig. 2

a Comparison of UCN1 and CRF2R in the G protein-bound structures in the side view. b Comparison of UCN1 and the TMD conformation in the G protein-bound structures in an extracellular view. c Comparison of the N terminus of UCN1 and the position of the ECL2 of CRF2R in the G protein-bound structures. d Comparison of the distinct conformational changes of ICL2 and the differences in the orientation of Gα in these three UCN1-CRF2R-G protein structures. e The binding pocket of UCN1(coral) in CRF2R (cornflower blue)-G11 (hot pink), UCN1(olive) in CRF2R (medium blue)-Go (dark khaki), and UCN1 (fire brick) in CRF2R (dark gray)-Gs (dark slate Blue). Many UCN1 side chains in the UCN1-CRF2R-G11 structure were truncated, whose rotamers shown here were based on the Rosetta-refined model. f Structural comparison of CRF2R H8 and Gβ1. g CRF2R H8 (cornflower blue)-Gβ1 (aquamarine) interface in the UCN1-CRF2R-G11 complex. The side chains of K372, and D379 of the receptor, and R42 and D312 of Gβ1were truncated in the structure, whose rotamers shown in this panel was from the Rosetta-refined model. h CRF2R H8 (medium blue)-Gβ1 (lime green) interface in the UCN1-CRF2R-Go complex. i CRF2R H8 (dark gray)-Gβ1 (teal) interface in the UCN1-CRF2R-Gs complex (PDB: 6PB1). The polar contacts are shown as purple dashed lines.

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