Fig. 3: Interaction patterns for the α5 helix of different G proteins. | Nature Communications

Fig. 3: Interaction patterns for the α5 helix of different G proteins.

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

Fig. 3: Interaction patterns for the α5 helix of different G proteins.The alternative text for this image may have been generated using AI.

a Comparison of the TMD conformation and the position of the Gα-α5 helix C terminus in the G protein-bound structures is shown in cartoon representation in an intracellular view. The red arrows indicate the α5 helix of G11 and Go shift away from TM5 or ICL2, compared to those of Gs. Structure of each CRF2R-G complex was superposed onto CRF2R-G11 based on the receptor component. CRF2R (cornflower blue)-G11 (hot pink), CRF2R (medium blue)-Go (dark khaki), CRF2R (dark gray)-Gs (dark slate blue) (PDB: 6PB1). b Comparison of the TM6 conformation in three complexes. c Sequence alignment of α5 in the different Gα proteins. The red box indicate the C-tail difference of G protein. d–f Binding pocket for the Gα-α5 C terminus. d UCN1-CRF2R-Gs (PDB: 6PB1); e UCN1-CRF2R-G11; f UCN1-CRF2R-Go.The receptors are shown in cartoon and surface representations in an intracellular view. g Interactions between CRF2R and Gα-α5 in UCN1-CRF2R-Gs (PDB: 6PB1). h Interactions between CRF2R and Gα-α5 in UCN1-CRF2R-G11. Many receptor side chains and those of K345, D346, and E355 on Gα-α5 were truncated in the structure, whose rotamers shown in this panel were from the Rosetta-refined model. i Interactions between CRF2R and Gα-α5 in UCN1-CRF2R-Go. The polar contacts are shown as purple dashed lines.

Back to article page