Daljit S. Bahia

TL;DR: A central role for hydrophobicity of this residue is defined in defining productive receptor-G protein interactions and the degree of activation of the forms of Gi1 alpha correlated strongly with the octanol/water partition coefficient of the amino acid at residue351.

TL;DR: In this article, the α-subunit of either Gi1 or Go1, containing point mutations to render them insensitive to the actions of pertussis toxin, were linked in-frame with the C-terminus of the receptor.

TL;DR: This is the first demonstration that the relative intrinsic activity of a series of agonists can be modified by a point mutation in a Gprotein rather than a receptor and indicates that the nature of a key contact site between a G protein and a receptor can selectively regulate partial agonist function.

TL;DR: The results demonstrate that the stability of the ternary complex between delta opioid receptor, G(i1)alpha and an agonist (but not antagonist) ligand is dependent upon the nature of residue(351) of the Gprotein and that this determines the effectiveness of information flow from the receptor to the G protein.

TL;DR: It is demonstrated that a fusion protein between a G’protein‐coupled receptor and an RGS protein is fully functional in providing both enhanced guanine nucleotide exchange and GTP hydrolysis of a coexpressed G”protein.