Robert J. Lefkowitz Born

The Nobel Prize in Chemistry 2012 was awarded jointly to Robert J. Lefkowitz
and Brian K.Kobilka "for studies of G-protein-coupled receptors"
學家羅伯特•萊夫科維茨(Robert J. Lefkowitz)和布賴恩•庫畢卡(K. Kobilka)共同分享了
Brian K. Kobilka
(G protein coupled receptors,簡稱GPCR)得獎,2人將
得獎的科學家為列夫科維茲(Robert J. Lefkowitz)和柯
比卡(Brain K. Kobilka),列夫科維茲生於1943年,現年
69歲,於美國杜克大學醫學中心(Duke University
Medical Center)的霍華德休斯醫學研究所(Howard
Hughes Medical Institute)擔任研究人員;柯比卡生於
(Stanford University School of Medicine)擔任研究人員。
在細胞膜上的受體家族,它與配體 (Ligand) 結合後產生
Born: 1955, Little Falls,
Affiliation at the time of
the award: Stanford
University School of
Medicine, Stanford, CA,
Robert J. Lefkowitz
Born: 1943, New York, NY,
Affiliation at the time of
the award: Howard
Hughes Medical Institute,
Duke University Medical
Center, Durham, NC, USA
Academician David Ma's
"Argonne’s connections to this year’s Chemistry Nobel Prize“
This is an image of a G-protein-coupled receptor signaling complex
whose structure was identified in 2011. The receptor is in magenta
while the different G protein subunits are colored green, red and
blue. Stanford biochemist Brian Kobilka shared the 2012 Nobel Prize
in Chemistry for his work in determining the structure of this
activated GPCR using X-rays provided by Argonne’s Advanced Photon
Figure 1. Cartoon of a cell with its interior (light blue) and exterior (blue), with their
different chemical compositions separated by a phospholipid bilayer. The bilayer
contains many proteins. Shown are two copies of a GPCR with specificity for a
diffusible ligand (yellow). The fraction of receptors with bound ligand is governed
by the ligand concentration. The receptor to the left is unoccupied and nonactivated, and the receptor to the right is occupied by a ligand, bound to a Gprotein (red), and activated. The ligand does not pass through the membrane; the
signal is transmitted by conformational changes in the receptor protein.
Figure 2. Left: Ternary complex model adapted from (17). A thermodynamic
cycle describes the formation of a complex of ligand (yellow), receptor
(blue) and G-protein (red). Right: Crystal structure of an active ternary
complex. Ribbon model drawn from the coordinates from file 3sn6.pdb (19)
using the software Molmol (20).
Figure 3. The prediction of seven helices in βAR is shown above rhodopsin.
The homologous amino acid sequences in helices five, six and seven are
aligned, and identities and similarities are coloured. Adapted from
reference 33.
Figure 4. Structural basis of the GPCR signalling mechanism. Non-activated
βAR (2bar.pdb) is shown to the left, and activated βAR bound to ligand and
G-protein (3sn6.pdb) to the right. At the top, the receptor in the membrane
is drawn with blue ribbon that traces the backbone. The bottom view is
from the inside of the cell membrane, with the receptor shown using a
space-filling model with hydrophobic side chains in dark blue.

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