Identification of the chloride-binding site in the human red and green color vision pigments

Wang, Zhiyan; Asenjo, Ana B.; Oprian, Daniel D.

doi:10.1021/bi00060a001

Cited by 153 publications

(159 citation statements)

References 41 publications

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“…In the long-wavelength cone visual pigments (green and red in human), a His residue at the position of Glu-181 in bovine rhodopsin has been demonstrated to bind a chloride ion, shifting the absorption maximum to the red (24). Presence of Wat2a in these chloride-binding pigments is suggested by our Fourier transform IR study on the chicken red pigment (25).…”

Section: Resultsmentioning

confidence: 58%

Functional role of internal water molecules in rhodopsin revealed by x-ray crystallography

Okada

Fujiyoshi

Silow

et al. 2002

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

683

899

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Activation of G protein-coupled receptors (GPCRs) is triggered and regulated by structural rearrangement of the transmembrane heptahelical bundle containing a number of highly conserved residues. In rhodopsin, a prototypical GPCR, the helical bundle accommodates an intrinsic inverse-agonist 11-cis-retinal, which undergoes photo-isomerization to the all-trans form upon light absorption. Such a trigger by the chromophore corresponds to binding of a diffusible ligand to other GPCRs. Here we have explored the functional role of water molecules in the transmembrane region of bovine rhodopsin by using x-ray diffraction to 2.6 Å. The structural model suggests that water molecules, which were observed in the vicinity of highly conserved residues and in the retinal pocket, regulate the activity of rhodopsin-like GPCRs and spectral tuning in visual pigments, respectively. To confirm the physiological relevance of the structural findings, we conducted single-crystal microspectrophotometry on rhodopsin packed in our three-dimensional crystals and show that its spectroscopic properties are similar to those previously found by using bovine rhodopsin in suspension or membrane environment. C ell surface membrane receptors mediate a variety of biological signaling processes that are triggered by a multitude of diffusible molecules or light in the case of visual pigments. G protein-coupled receptors (GPCRs), including the rhodopsinlike family as a dominant subgroup, are the largest group of membrane receptors. Many of the members are considered as primary drug targets for various medical and pharmacological interventions. These receptors appear to be activated by a mechanism involving common heptahelical transmembrane architecture that undergoes major rearrangement upon signal reception, resulting in activation of the heterotrimeric G protein molecules.Rhodopsin from retinal rod cells mediates scotopic vision. It is a unique member among GPCRs in that it contains an intrinsic inverse-agonist, the 11-cis-retinal. Photon absorption results in retinal isomerization to the all-trans configuration, which drives the protein to the active metarhodopsin form (M II) (1). Visual pigments mediating color vision in cone cells share a common mechanism to evoke a cellular signaling cascade (2) through interaction between the M II state and the G protein. A view of the seven helices of bovine rhodopsin was provided by electron crystallography in 1993 (3), and an x-ray crystallographic study recently determined its structure at 2.8-Å resolution (4). This structure provided the template model at high resolution for the rhodopsin-like GPCRs and has been further refined at the same resolution (5).The 11-cis-retinal chromophore is covalently bound to Lys-296 in transmembrane helix VII by a protonated Schiff base linkage, which is stabilized by the negatively charged counterion Glu-113 in helix III. Disruption of this salt bridge (6) upon proton transfer is thought to trigger conformational changes in rhodopsin (7), which are necessary for G protein ...

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Section: Resultsmentioning

confidence: 58%

Functional role of internal water molecules in rhodopsin revealed by x-ray crystallography

Okada

Fujiyoshi

Silow

et al. 2002

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

683

899

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“…The latter reaction clearly demonstrates that the proteins contain the histidine tag and therefore are full-length. Remarkably, earlier functional expression studies [6,7,16,19,20] did not present immunochemical identification of the cone pigments. Since the assembly of separate polypeptide fragments, corresponding to proteolytically cleaved rhodopsin, can produce a spectrally intact visual pigment [21], our results represent the first immunoblot identification of full-length mammalian cone pigments.…”

Section: Discussionmentioning

confidence: 85%

“…Because of their low abundance in mamnalian retinas, functional expression of recombinant cone pignents offers a potential way to investigate these proteins in nore detail. So far, functional expression has been achieved in nammalian cell lines and provided information on basic specral properties of wild type [6,7] and on spectral tuning in nutant pigments [ 16,19,20].…”

Section: Discussionmentioning

confidence: 99%

Functional expression of human cone pigments using recombinant baculovirus: compatibility with histidine tagging and evidence for N‐glycosylation

Vissers

DeGrip

1996

FEBS Letters

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Mammalian color vision is mediated by fight-sensitive pigments in retinal cone cells. Biochemical studies on native mammalian cone visual pigments are seriously hampered by their low levels and instability. We describe a novel approach for their functional expression, employing the baculovirus system in combination with histidine tagging to allow future purification and structural analysis. The human red and green cone pigments are produced in relatively large amounts and can be detected by immunocytochemistry as well as by immunoblotting. Histidine tagging has no significant effect on the absorhance maxima. The first evidence is presented that these pigments are N-glycosylated.

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“…3, but the site 181 is folded into the TM region (Palczewski et al, 2000). In addition, H181, but not Y181, binds to chloride and H181Y may cause a structural change, resulting in a significant l max -shift (Wang et al, 1993). Thus, to explain the spectral tuning of all LWS/ MWS pigments, it is necessary to consider amino acid differences at five sites, 164, 181, 261, 269, and 292 (Fig.…”

Section: Red-green Color Visionmentioning

confidence: 99%

Molecular evolution of color vision in vertebrates

Yokoyama

2002

Gene

261

231

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Visual systems of vertebrates exhibit a striking level of diversity, reflecting their adaptive responses to various color environments. The photosensitive molecules, visual pigments, can be synthesized in vitro and their absorption spectra can be determined. Comparing the amino acid sequences and absorption spectra of various visual pigments, we can identify amino acid changes that have modified the absorption spectra of visual pigments. These hypotheses can then be tested using the in vitro assay. This approach has been a powerful tool in elucidating not only the molecular bases of color vision, but the processes of adaptive evolution at the molecular level. q

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Identification of the chloride-binding site in the human red and green color vision pigments

Cited by 153 publications

References 41 publications

Functional role of internal water molecules in rhodopsin revealed by x-ray crystallography

Functional role of internal water molecules in rhodopsin revealed by x-ray crystallography

Functional expression of human cone pigments using recombinant baculovirus: compatibility with histidine tagging and evidence for N‐glycosylation

Molecular evolution of color vision in vertebrates

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