Crystal structure of a GA protein βγdimer at 2.1 Å resolution View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1996-01

AUTHORS

John Sondek, Andrew Bohm, David G. Lambright, Heidi E. Hamm, Paul B. Sigler

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. More... »

PAGES

369-374

Journal

TITLE

Nature

ISSUE

6563

VOLUME

379

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/379369a0

DOI

http://dx.doi.org/10.1038/379369a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1041590546

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8552196


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