Regulation of retinal transducin by C-terminal peptides of rhodopsin
نویسندگان
چکیده
منابع مشابه
Regulation of retinal transducin by C-terminal peptides of rhodopsin.
Transducin is a multi-subunit guanine-nucleotide-binding protein that mediates signal coupling between rhodopsin and cyclic GMP phosphodiesterase in retinal rod outer segments. Whereas the T alpha subunit of transducin binds guanine nucleotides and is the activator of the phosphodiesterase, the T beta gamma subunit may function to link physically T alpha with photolysed rhodopsin. In order to d...
متن کاملDefining the interface between the C-terminal fragment of alpha-transducin and photoactivated rhodopsin.
A novel combination of experimental data and extensive computational modeling was used to explore probable protein-protein interactions between photoactivated rhodopsin (R*) and experimentally determined R*-bound structures of the C-terminal fragment of alpha-transducin (Gt(alpha)(340-350)) and its analogs. Rather than using one set of loop structures derived from the dark-adapted rhodopsin sta...
متن کاملRhodopsin-transducin interface: studies with conformationally constrained peptides.
To probe the interaction between transducin (G(t)) and photoactivated rhodopsin (R*), 14 analog peptides were designed and synthesized restricting the backbone of the R*-bound structure of the C-terminal 11 residues of G(t)alpha derived by transferred nuclear Overhauser effect (TrNOE) NMR. Most of the analogs were able to bind R*, supporting the TrNOE structure. Improved affinities of constrain...
متن کاملNMR analysis of rhodopsin–transducin interactions
Heterotrimeric G-protein activation by an agonist-stimulated G-protein coupled receptor (R*) requires the propagation of structural signals from the receptor interacting surfaces to the guanine nucleotide-binding pocket. Employing high-resolution NMR methods, we are probing heterotrimer-associated and rhodopsin-stimulated changes in an isotope-labeled G-protein alpha-subunit (G(alpha)). A key a...
متن کاملOpsin/all-trans-retinal complex activates transducin by different mechanisms than photolyzed rhodopsin.
In rhodopsin, the 11-cis-retinal chromophore forms a complex with Lys296 of opsin via a protonated Schiff base. Absorption of light initiates the activation of rhodopsin by cis/trans photoisomerization of retinal. Thermal relaxation through different intermediates leads into the metarhodopsin states which bind and activate transducin (Gt) and rhodopsin kinase (RK). all-trans-Retinal also recomb...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1985
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj2320669