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Contents |
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* Residue conservation analysis
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DOI no:
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Science
289:739-745
(2000)
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PubMed id:
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Crystal structure of rhodopsin: A G protein-coupled receptor.
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K.Palczewski,
T.Kumasaka,
T.Hori,
C.A.Behnke,
H.Motoshima,
B.A.Fox,
I.Le Trong,
D.C.Teller,
T.Okada,
R.E.Stenkamp,
M.Yamamoto,
M.Miyano.
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ABSTRACT
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Heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptors
(GPCRs) respond to a variety of different external stimuli and activate G
proteins. GPCRs share many structural features, including a bundle of seven
transmembrane alpha helices connected by six loops of varying lengths. We
determined the structure of rhodopsin from diffraction data extending to 2.8
angstroms resolution. The highly organized structure in the extracellular
region, including a conserved disulfide bridge, forms a basis for the
arrangement of the seven-helix transmembrane motif. The ground-state
chromophore, 11-cis-retinal, holds the transmembrane region of the protein in
the inactive conformation. Interactions of the chromophore with a cluster of key
residues determine the wavelength of the maximum absorption. Changes in these
interactions among rhodopsins facilitate color discrimination. Identification of
a set of residues that mediate interactions between the transmembrane helices
and the cytoplasmic surface, where G-protein activation occurs, also suggests a
possible structural change upon photoactivation.
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Selected figure(s)
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Figure 2.
Fig. 2. Ribbon drawings of rhodopsin. (A) Parallel to the plane
of the membrane (stereoview). A view into the membrane plane is
seen from the cytoplasmic (B) and intradiscal side (C) of the
membrane.
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Figure 5.
Fig. 5. Structural details for four regions in rhodopsin. (A)
The E-II loop near the disulfide bridge connecting Cys110 and
Cys187, viewed from extracellular side. (B) The C-IV cytoplasmic
loop from Lys311 to Leu321 forming a short amphiphillic helix
(H-VIII). (C) Interhelical hydrogen bonds mediated by a highly
conserved Asn55, connecting H-I, H-II, and H-VII, and by Asn78
for H-II, H-III, and H-IV. (D) The tripeptide region,
Glu134-Arg135-Tyr136, known as a (D/E)R(Y/W) motif located near
the cytoplasmic end of H-III.
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The above figures are
reprinted
by permission from the AAAs:
Science
(2000,
289,
739-745)
copyright 2000.
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Figures were
selected
by an automated process.
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PubMed id
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