"High-resolution crystal structure of an engineered human
beta(2)-adrenergic G protein-coupled receptor," by Vadim Cherezov
and 10 others, Science, 318(5854): 1258-65, 23 November 2007.
[Authors' affiliations: Scripps Research Institute, La Jolla, CA; Stanford
University, CA]
Abstract: "Heterotrimeric guanine nucleotide-binding protein (G
protein)-coupled receptors constitute the largest family of eukaryotic
signal transduction proteins that communicate across the membrane. We
report the crystal structure of a human beta(2)-adrenergic receptor-T4
lysozyme fusion protein bound to the partial inverse agonist carazolol at
2.4 angstrom resolution. The structure provides a high-resolution view of a
human G protein-coupled receptor bound to a diffusible ligand.
Ligand-binding site accessibility is enabled by the second extracellular
loop, which is held out of the binding cavity by a pair of closely spaced
disulfide bridges and a short helical segment within the loop. Cholesterol,
a necessary component for crystallization, mediates an intriguing parallel
association of receptor molecules in the crystal lattice. Although the
location of carazolol in the beta(2)-adrenergic receptor is very similar to
that of retinal in rhodopsin, structural differences in the ligand-binding
site and other regions highlight the challenges in using rhodopsin as a
template model for this large receptor family."
This 2007 report from Science was cited 42 times in
current journal articles indexed by Clarivate during July-August
2009. Only two other biology papers published in the last two years, aside
from reviews, garnered higher citation totals during that two-month period.
Prior to the most recent bimonthly count, citations to the paper have
accrued as follows:
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