Abstract
MANY signalling cascades use seven-helical transmembrane receptors coupled to heterotrimeric G proteins (Gαβγ) to convert extracellular signals into intracellular responses1. Upon nucleotide exchange catalysed by activated receptors, heterotrimers dissociate into GTP-bound Gα subunits and Gβγ dimers, either of which can modulate many downstream effectors2,3. Here we use multiwavelength anomalous diffraction data to solve the crystal structure of the βγ dimer of the G protein transducin. The β-subunit is primarily a seven-bladed β-propeller that is partially encircled by an extended γ-subunit. The β-propeller, which contains seven structurally similar WD repeats, defines the stereochemistry of the WD repeat and the probable architecture of all WD-repeat-containing domains. The structure details interactions between G protein β- and γ-subunits and highlights regions implicated in effector modulation for the conserved family of G protein βγ dimers.
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Sondek, J., Bohm, A., Lambright, D. et al. Crystal structure of a GA protein βγdimer at 2.1 Å resolution. Nature 379, 369–374 (1996). https://doi.org/10.1038/379369a0
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DOI: https://doi.org/10.1038/379369a0
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