The structure of bovine rhodopsin

Hargrave, Paul A.; McDowell, J. Hugh; Curtis, Donna R.; Wang, Janet K.; Juszczak, Elizabeth; Fong, Shao-Ling; Rao, Jayasimha; Argos, Patrick

doi:10.1007/bf00535659

Cited by 481 publications

(278 citation statements)

References 11 publications

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“…Its role is in marked contrast to the roles of Lys-296 and Glu-113, which are essential for the basic function (photoreception) of the vertebrate visual pigments. Specifically, these residues are responsible for chromophore binding (16,37,38) and its stabilization as a counterion (22,23,39), respectively. The role of the amino acid residue at position 122 is relatively similar to the roles of the amino acid residues that tune the spectral sensitivity of visual pigments and thus form a molecular basis of color vision (10).…”

Section: Discussionmentioning

confidence: 99%

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Single amino acid residue as a functional determinant of rod and cone visual pigments

Imai

Kojima

Oura

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

137

141

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The visual transduction processes in rod and cone photoreceptor cells begin with photon absorption by the different types of visual pigments. Cone visual pigments exhibit faster regeneration from 11-cis-retinal and opsin and faster decay of physiologically active intermediate (meta II) than does the rod visual pigment, rhodopsin, as expected, due to the functional difference between rod and cone photoreceptor cells. To identify the amino acid residue(s) responsible for the difference in molecular properties between rod and cone visual pigments, we selected three amino acid positions (64, 122, and 150), where cone visual pigments have amino acid residues electrically different from those of rhodopsin, and prepared mutants of rhodopsin and chicken greensensitive cone visual pigment. The results showed that the replacement of Glu-122 of rhodopsin by the residue containing green-or red-sensitive cone pigment converted rhodopsin's rates of regeneration and meta II decay into those of the respective cone pigments, whereas the introduction of Glu-122 into green-sensitive cone visual pigment changed the rates of these processes into rates similar to those of rhodopsin. Furthermore, exchange of the residue at position 122 between rhodopsin and chicken green-sensitive cone pigment interchanges their efficiencies in activating retinal G protein transducin. Thus, the amino acid residue at position 122 is a functional determinant of rod and cone visual pigments.

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Section: Discussionmentioning

confidence: 99%

“…The standard deviations were estimated from three independent experiments using different preparations. (16). Amino acid positions indicated with white circles are those in which rhodopsin and the four types of cone visual pigments have residues similar in electric properties.…”

Section: Methodsmentioning

confidence: 99%

Single amino acid residue as a functional determinant of rod and cone visual pigments

Imai

Kojima

Oura

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

137

141

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“…Perhaps we should call this pathway prototypical , since it was the first G-protein receptor cascade whose elements were completely identified and mechanism understood. The visual pigment rhodopsin was the first G-protein-coupled receptor whose amino acid sequence was determined (12)(13)(14) and, as yet, the only one whose structure has been solved by X-ray crystallography. (15,16) Rhodopsin in a vertebrate rod consists of two parts: a protein called opsin and a small molecular-weight chromophore called 11-cis retinal, which is bound covalently to a lysine of the opsin.…”

Section: Transduction In Vertebrate Photoreceptorsmentioning

confidence: 99%

Why photoreceptors die (and why they don't)

Fain

2006

BioEssays

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Light can kill the photoreceptors of the eye, not only very bright direct sunlight, but more moderate illumination if the light is present continuously. Recent experiments show that rod apoptosis can be triggered by strong and constant activation of transduction, and that death can be prevented if transduction is inhibited even though the eye is illuminated. Vitamin A deficiency and genetically inherited diseases, such as some forms of retinitis pigmentosa and Leber congenital amaurosis, appear to kill like this: transduction is activated at a high rate and continuously, and this causes the rods to die. Why does transduction kill? Our best guess is that continuous activation produces a prolonged lowering of the Ca2+ concentration, which is also thought to kill neurons in tissue culture and during the development of the nervous system. To prevent death in constant light, rods have evolved protective mechanisms including modulation of channels and ion transport to keep the Ca2+ from going too low. Prolonged light exposure also causes migration of transduction proteins from one part of the cell to another and a reversible shortening of the rod outer segments, the part of the cell that contains the pigment rhodopsin. All of these mechanisms are at work in the normal eye to reduce transduction and prevent the Ca2+ concentration from dropping too low for too long a time. That most of us retain our vision our entire lives is a testament to their effectiveness. BioEssays 28: 344–354, 2006. © 2006 Wiley Periodicals, Inc.

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“…The fact that the peptide sequence of bovine rhodopsin has been resolved (expect for minor details) and that its secondary structure has been predicted (Ovchinnikov et al 1982;Hargrave et al 1983 -this issue) may be called this year's most exciting (and perhaps also most painstaking) step forward in visual pigment research (Dratz and Hargrave 1983). The thermochemical changes [2] occurring in the visual molecule after light absorption go through a series of stages.…”

Section: The Visual Pigmentmentioning

confidence: 99%