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Light-induced conformational change in rhodopsin detected by modification of G-protein binding, GTP gamma S binding and cGMP phosphodiesterase activation.
- Source :
-
FEBS letters [FEBS Lett] 1985 Feb 11; Vol. 181 (1), pp. 184-8. - Publication Year :
- 1985
-
Abstract
- CNBr treatment of rod outer segments was performed in dark and in light conditions. With the subsequent modified rhodopsin and opsin the cGMP phosphodiesterase activation system was reconstituted. The recombination systems exhibited greatly reduced G-protein binding, GTP gamma S binding and cGMP phosphodiesterase activation. The reduction in activity of these three steps of the PDE activation cascade is most significant with modified opsin and is shown to be due to its inability to bind the G alpha subunit. The correlation between the localization of CNBr cleavage in dark and light conditions and these results is strongly indicative that a light-induced conformational change occurs in two extradiscal regions of rhodopsin.
- Subjects :
- Animals
Cattle
Cyanogen Bromide pharmacology
Electrophoresis, Polyacrylamide Gel
Enzyme Activation
Guanosine 5'-O-(3-Thiotriphosphate)
Guanosine Triphosphate metabolism
Light
Protein Conformation
Rod Cell Outer Segment analysis
3',5'-Cyclic-GMP Phosphodiesterases metabolism
GTP-Binding Proteins metabolism
Guanosine Triphosphate analogs & derivatives
Retinal Pigments analysis
Rhodopsin analysis
Thionucleotides metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0014-5793
- Volume :
- 181
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- FEBS letters
- Publication Type :
- Academic Journal
- Accession number :
- 2982652
- Full Text :
- https://doi.org/10.1016/0014-5793(85)81139-x