Extended Data Fig. 5: Rotational opening of the α-helical domain during G-protein activation by GPCRs. | Nature Structural & Molecular Biology

Extended Data Fig. 5: Rotational opening of the α-helical domain during G-protein activation by GPCRs.

From: Structural basis and mechanism of activation of two different families of G proteins by the same GPCR

Extended Data Fig. 5

(a) Structure of Gαi in the complex of β1-AR–Gi shows the rotational opening of the α-helical domain away from the Ras-like domain. (b) Comparison of the structures of Gαi in the complex of β1-AR–Gi (in green and orange) and in the inactive GDP-bound Gi crystal structure (in gray; PDB: 1GG2). (c) View from the receptor towards the cytoplasmic end shows the rotation of the α-helical domain from the position in inactive Gi (in gray) to the location in the β1-AR–Gi complex (in orange). (d) View from Gβγ towards the Ras-like domain shows the position of the α-helical domain relative to Gβ. (e and f) Comparisons of the locations of the α-helical domains in the complexes of β2-AR–Gs (PDB: 3SN6), β1-AR–Gs (PDB: 7JJO), rhodopsin–Gi (PDB: 6CMO), and β1-AR–Gi (this paper).

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