Crystal structure of a G-protein beta gamma dimer at 2.1A resolution.

Sondek J, Bohm A, Lambright DG, Hamm HE, Sigler PB
Nature. 1996 379 (6563): 369-74

PMID: 8552196 · DOI:10.1038/379369a0

Many signalling cascades use seven-helical transmembrane receptors coupled to heterotrimeric G proteins (G alpha beta gamma) to convert extracellular signals into intracellular responses. Upon nucleotide exchange catalysed by activated receptors, heterotrimers dissociate into GTP-bound G alpha subunits and G beta gamma dimers, either of which can modulate many downstream effectors. Here we use multiwavelength anomalous diffraction data to solve the crystal structure of the beta gamma dimer of the G protein transducin. The beta-subunit is primarily a seven-bladed beta-propeller that is partially encircled by an extended gamma-subunit. The beta-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 beta- and gamma-subunits and highlights regions implicated in effector modulation for the conserved family of G protein beta gamma dimers.

MeSH Terms (10)

Amino Acid Sequence Animals Crystallography, X-Ray Humans Models, Molecular Molecular Sequence Data Protein Conformation Retinal Rod Photoreceptor Cells Sequence Homology, Amino Acid Transducin

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