1tbg
BETA-GAMMA DIMER OF THE HETEROTRIMERIC G-PROTEIN TRANSDUCIN
|
OverviewOverview
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.
About this StructureAbout this Structure
1TBG is a Protein complex structure of sequences from Bos taurus. The following page contains interesting information on the relation of 1TBG with [G Proteins]. Full crystallographic information is available from OCA.
ReferenceReference
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 Jan 25;379(6563):369-74. PMID:8552196
Page seeded by OCA on Mon Nov 12 19:23:12 2007