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PDBsum entry 1kpw
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Membrane protein
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PDB id
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1kpw
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DOI no:
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Biochim Biophys Acta
1565:168-182
(2002)
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PubMed id:
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Crystal structure of rhodopsin: a template for cone visual pigments and other G protein-coupled receptors.
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R.E.Stenkamp,
S.Filipek,
C.A.Driessen,
D.C.Teller,
K.Palczewski.
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ABSTRACT
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The crystal structure of rhodopsin has provided the first three-dimensional
molecular model for a G-protein-coupled receptor (GPCR). Alignment of the
molecular model from the crystallographic structure with the helical axes seen
in cryo-electron microscopic (cryo-EM) studies provides an opportunity to
investigate the properties of the molecule as a function of orientation and
location within the membrane. In addition, the structure provides a starting
point for modeling and rational experimental approaches of the cone pigments,
the GPCRs in cone cells responsible for color vision. Homology models of the
cone pigments provide a means of understanding the roles of amino acid sequence
differences that shift the absorption maximum of the retinal chromophore in the
environments of different opsins.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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J.C.Gardner,
T.R.Webb,
N.Kanuga,
A.G.Robson,
G.E.Holder,
A.Stockman,
C.Ripamonti,
N.D.Ebenezer,
O.Ogun,
S.Devery,
G.A.Wright,
E.R.Maher,
M.E.Cheetham,
A.T.Moore,
M.Michaelides,
and
A.J.Hardcastle
(2010).
X-linked cone dystrophy caused by mutation of the red and green cone opsins.
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Am J Hum Genet,
87,
26-39.
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A.Altun,
S.Yokoyama,
and
K.Morokuma
(2009).
Color tuning in short wavelength-sensitive human and mouse visual pigments: ab initio quantum mechanics/molecular mechanics studies.
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J Phys Chem A,
113,
11685-11692.
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P.S.Park,
K.T.Sapra,
B.Jastrzebska,
T.Maeda,
A.Maeda,
W.Pulawski,
M.Kono,
J.Lem,
R.K.Crouch,
S.Filipek,
D.J.Müller,
and
K.Palczewski
(2009).
Modulation of molecular interactions and function by rhodopsin palmitylation.
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Biochemistry,
48,
4294-4304.
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S.P.Thirumuruganandham,
and
H.M.Urbassek
(2009).
Low-frequency vibrational modes and infrared absorbance of red, blue and green opsin.
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J Mol Model,
15,
959-969.
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N.Yanamala,
K.C.Tirupula,
and
J.Klein-Seetharaman
(2008).
Preferential binding of allosteric modulators to active and inactive conformational states of metabotropic glutamate receptors.
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BMC Bioinformatics,
9,
S16.
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D.Marsh
(2007).
Lateral pressure profile, spontaneous curvature frustration, and the incorporation and conformation of proteins in membranes.
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Biophys J,
93,
3884-3899.
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R.C.Baraas,
J.Carroll,
K.L.Gunther,
M.Chung,
D.R.Williams,
D.H.Foster,
and
M.Neitz
(2007).
Adaptive optics retinal imaging reveals S-cone dystrophy in tritan color-vision deficiency.
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J Opt Soc Am A Opt Image Sci Vis,
24,
1438-1447.
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A.Dreuw
(2006).
Quantum chemical methods for the investigation of photoinitiated processes in biological systems: theory and applications.
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Chemphyschem,
7,
2259-2274.
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B.E.Kane,
B.Svensson,
and
D.M.Ferguson
(2006).
Molecular recognition of opioid receptor ligands.
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AAPS J,
8,
E126-E137.
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R.E.Stenkamp,
D.C.Teller,
and
K.Palczewski
(2005).
Rhodopsin: a structural primer for G-protein coupled receptors.
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Arch Pharm (Weinheim),
338,
209-216.
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S.Balasubramanian,
Y.Xia,
E.Freinkman,
and
M.Gerstein
(2005).
Sequence variation in G-protein-coupled receptors: analysis of single nucleotide polymorphisms.
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Nucleic Acids Res,
33,
1710-1721.
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Z.Wang,
X.H.Wen,
Z.Ablonczy,
R.K.Crouch,
C.L.Makino,
and
J.Lem
(2005).
Enhanced shutoff of phototransduction in transgenic mice expressing palmitoylation-deficient rhodopsin.
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J Biol Chem,
280,
24293-24300.
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J.M.Janz,
and
D.L.Farrens
(2004).
Role of the retinal hydrogen bond network in rhodopsin Schiff base stability and hydrolysis.
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J Biol Chem,
279,
55886-55894.
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K.Suda,
S.Filipek,
K.Palczewski,
A.Engel,
and
D.Fotiadis
(2004).
The supramolecular structure of the GPCR rhodopsin in solution and native disc membranes.
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Mol Membr Biol,
21,
435-446.
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S.U.Miedlich,
L.Gama,
K.Seuwen,
R.M.Wolf,
and
G.E.Breitwieser
(2004).
Homology modeling of the transmembrane domain of the human calcium sensing receptor and localization of an allosteric binding site.
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J Biol Chem,
279,
7254-7263.
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T.Huber,
A.V.Botelho,
K.Beyer,
and
M.F.Brown
(2004).
Membrane model for the G-protein-coupled receptor rhodopsin: hydrophobic interface and dynamical structure.
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Biophys J,
86,
2078-2100.
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D.C.Teller,
R.E.Stenkamp,
and
K.Palczewski
(2003).
Evolutionary analysis of rhodopsin and cone pigments: connecting the three-dimensional structure with spectral tuning and signal transfer.
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FEBS Lett,
555,
151-159.
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G.Bhave,
B.M.Nadin,
D.J.Brasier,
K.S.Glauner,
R.D.Shah,
S.F.Heinemann,
F.Karim,
and
R.W.Gereau
(2003).
Membrane topology of a metabotropic glutamate receptor.
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J Biol Chem,
278,
30294-30301.
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M.Natochin,
K.G.Gasimov,
M.Moussaif,
and
N.O.Artemyev
(2003).
Rhodopsin determinants for transducin activation: a gain-of-function approach.
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J Biol Chem,
278,
37574-37581.
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S.Filipek,
D.C.Teller,
K.Palczewski,
and
R.Stenkamp
(2003).
The crystallographic model of rhodopsin and its use in studies of other G protein-coupled receptors.
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Annu Rev Biophys Biomol Struct,
32,
375-397.
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S.Filipek,
R.E.Stenkamp,
D.C.Teller,
and
K.Palczewski
(2003).
G protein-coupled receptor rhodopsin: a prospectus.
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Annu Rev Physiol,
65,
851-879.
|
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T.Mirzadegan,
G.Benkö,
S.Filipek,
and
K.Palczewski
(2003).
Sequence analyses of G-protein-coupled receptors: similarities to rhodopsin.
|
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Biochemistry,
42,
2759-2767.
|
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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}
}
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