Abstract
Incubation of opsin with synthetic 6-s-locked retinoids 2a and 2b only led to pigment formation from the alpha-locked 2a, the CD spectrum of which was similar to that of native rhodopsin (Rh). This establishes that the 6-s-bond of the chromophore in rhodopsin is cis, and that its helicity is negative. Earlier cross-linking studies showed that the 11-cis to all-trans photoisomerization occurring in the batho-Rh to lumi-Rh conversion induces a flip over of the side carrying the ring moiety. The GTP-binding assay of pigment Rh-(2a), incorporating retinal analogue 2a, has shown that its activity is 80% that of the native pigment. That is, the overall conformation around the 6-s bond is retained in the steps leading to G-protein activation.
| Original language | English |
|---|---|
| Pages (from-to) | 4198-4204 |
| Number of pages | 7 |
| Journal | Chemistry - A European Journal |
| Volume | 7 |
| Issue number | 19 |
| DOIs | |
| Publication status | Published - 2001 Oct 1 |
| Externally published | Yes |
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Keywords
- Chirality
- Circular dichroism
- Conformation analysis
- Receptors
- Retinal
- Rhodopsin
ASJC Scopus subject areas
- Chemistry(all)
Cite this
On the bioactive conformation of the rhodopsin chromophore : Absolute sense of twist around the 6-s-cis bond. / Fujimoto, Yukari; Ishihara, Jun; Maki, Shojiro; Fujioka, Naoko; Wang, Tao; Furuta, Takumi; Fishkin, Nathan; Borhan, Babak; Berova, Nina; Nakanishi, Koji.
In: Chemistry - A European Journal, Vol. 7, No. 19, 01.10.2001, p. 4198-4204.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - On the bioactive conformation of the rhodopsin chromophore
T2 - Absolute sense of twist around the 6-s-cis bond
AU - Fujimoto, Yukari
AU - Ishihara, Jun
AU - Maki, Shojiro
AU - Fujioka, Naoko
AU - Wang, Tao
AU - Furuta, Takumi
AU - Fishkin, Nathan
AU - Borhan, Babak
AU - Berova, Nina
AU - Nakanishi, Koji
PY - 2001/10/1
Y1 - 2001/10/1
N2 - Incubation of opsin with synthetic 6-s-locked retinoids 2a and 2b only led to pigment formation from the alpha-locked 2a, the CD spectrum of which was similar to that of native rhodopsin (Rh). This establishes that the 6-s-bond of the chromophore in rhodopsin is cis, and that its helicity is negative. Earlier cross-linking studies showed that the 11-cis to all-trans photoisomerization occurring in the batho-Rh to lumi-Rh conversion induces a flip over of the side carrying the ring moiety. The GTP-binding assay of pigment Rh-(2a), incorporating retinal analogue 2a, has shown that its activity is 80% that of the native pigment. That is, the overall conformation around the 6-s bond is retained in the steps leading to G-protein activation.
AB - Incubation of opsin with synthetic 6-s-locked retinoids 2a and 2b only led to pigment formation from the alpha-locked 2a, the CD spectrum of which was similar to that of native rhodopsin (Rh). This establishes that the 6-s-bond of the chromophore in rhodopsin is cis, and that its helicity is negative. Earlier cross-linking studies showed that the 11-cis to all-trans photoisomerization occurring in the batho-Rh to lumi-Rh conversion induces a flip over of the side carrying the ring moiety. The GTP-binding assay of pigment Rh-(2a), incorporating retinal analogue 2a, has shown that its activity is 80% that of the native pigment. That is, the overall conformation around the 6-s bond is retained in the steps leading to G-protein activation.
KW - Chirality
KW - Circular dichroism
KW - Conformation analysis
KW - Receptors
KW - Retinal
KW - Rhodopsin
UR - http://www.scopus.com/inward/record.url?scp=0035476603&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0035476603&partnerID=8YFLogxK
U2 - 10.1002/1521-3765(20011001)7:19<4198::AID-CHEM4198>3.0.CO;2-X
DO - 10.1002/1521-3765(20011001)7:19<4198::AID-CHEM4198>3.0.CO;2-X
M3 - Article
VL - 7
SP - 4198
EP - 4204
JO - Chemistry - A European Journal
JF - Chemistry - A European Journal
SN - 0947-6539
IS - 19
ER -