منابع مشابه
Enantioselective binding of an 11-cis-locked cyclopropyl retinal. The conformation of retinal in bovine rhodopsin.
[formula: see text] The conformation of the retinal chromophore in rhodopsin is central for understanding the visual transduction process. The absolute twist around the 12-s bond of the chromophore in rhodopsin has been determined by studies with 11-cis-locked 11,12-cyclopropylretinal analogues (11S,12R)-2 and (11R,12S)-3, enantioselectively synthesized with the aid of an enzyme. The finding th...
متن کاملA rhodopsin exhibiting binding ability to agonist all-trans-retinal.
Rhodopsins are the members of the family of G protein-coupled receptors that have diverged from ligand-binding receptors into photoreceptive pigments. Vertebrate rhodopsins are able to bind the inverse agonist 11-cis-retinal but are unable to bind the agonist all-trans-retinal, indicating that vertebrate rhodopsin changed its binding ability during the course of molecular evolution. Here, we sh...
متن کاملArrestin-rhodopsin interaction. Multi-site binding delineated by peptide inhibition.
Visual arrestin modulates the intracellular response of retinal rod cells to light by specifically binding to the phosphorylated light-activated form of the photoreceptor rhodopsin (P-Rh*). In order to characterize the molecular interaction between rhodopsin and arrestin, we have studied the ability of synthetic peptides from the proposed cytoplasmic loops of rhodopsin to inhibit arrestin bindi...
متن کاملRetinal Flip in Rhodopsin Activation?
Rhodopsin is a well-characterized structural model of a G protein-coupled receptor. Photoisomerization of the covalently bound retinal triggers activation. Surprisingly, the x-ray crystal structure of the active Meta-II state has a 180° rotation about the long-axis of the retinal polyene chain. Unbiased microsecond-timescale all-atom molecular dynamics simulations show that the retinal cofactor...
متن کاملOcular manifestations in autosomal dominant retinitis pigmentosa with a Lys-296-Glu rhodopsin mutation at the retinal binding site.
A lysine to glutamic acid substitution at codon 296 in the rhodopsin gene has been reported in a family with autosomal dominant retinitis pigmentosa. This mutation is of particular functional interest as this lysine molecule is the binding site of 11-cis-retinal. The clinical features of a family with this mutation have not been reported previously. We examined 14 patients with autosomal domina...
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ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 1991
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.31.121