"High-resolution crystal structure of an engineered human bet
(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 43
times in current journal articles indexed by Clarivate
during September-October 2008. Only one other biology paper published in
the last two years, aside from reviews, garnered a higher number of
citations during that two-month period. Prior to the most recent bimonthly
count, citations to the paper have accrued as follows:
SOURCE:
Hot Papers
Database (Included with a subscription to the print newsletter
Science
Watch®, available from the
Research Services
Group of
Thomson
Reuters. Packaged on a CD that is mailed
with each Science Watch issue, the Hot Papers
Database contains data on hundreds of highly cited papers published during
the last two years. User interface permits searching by author,
organization, journal, field, and more. Total citations, as well as
citations accrued during successive bimonthly periods, can be assessed and
graphed. An updated CD containing the most recent bimonthly data is mailed
with every new issue of Science Watch, six times a
year. The CD also includes an electronic version of the Science
Watch issue in HTML format, for personal desktop
access.