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pubmed-article:11301033pubmed:abstractTextRegeneration of visual pigments of vertebrate rod and cone photoreceptors occurs by the initial noncovalent binding of 11-cis-retinal to opsin, followed by the formation of a covalent bond between the ligand and the protein. Here, we show that the noncovalent interaction between 11-cis-retinal and opsin affects the rate of dark adaptation. In rods, 11-cis-retinal produces a transient activation of the phototransduction cascade that precedes sensitivity recovery, thus slowing dark adaptation. In cones, 11-cis-retinal immediately deactivates phototransduction. Thus, the initial binding of the same ligand to two very similar G protein receptors, the rod and cone opsins, activates one and deactivates the other, contributing to the remarkable difference in the rates of rod and cone dark adaptation.lld:pubmed
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pubmed-article:11301033pubmed:authorpubmed-author:CornwallM CMClld:pubmed
pubmed-article:11301033pubmed:authorpubmed-author:CrouchR KRKlld:pubmed
pubmed-article:11301033pubmed:authorpubmed-author:KefalovV JVJlld:pubmed
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pubmed-article:11301033pubmed:dateRevised2008-11-21lld:pubmed
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pubmed-article:11301033pubmed:articleTitleRole of noncovalent binding of 11-cis-retinal to opsin in dark adaptation of rod and cone photoreceptors.lld:pubmed
pubmed-article:11301033pubmed:affiliationDepartment of Physiology, Boston University School of Medicine, 715 Albany Street, Boston, MA 02118, USA. vkefalov@jhmi.edulld:pubmed
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