Study of the shape of the binding site of bovine opsin using 10-substituted retinal isomers.
The 9-cis, 11-cis, 13-cis, and all-trans isomers of 10-fluoro-, 10-chloro-, 10-methyl-, and 10-ethylretinals have been prepared and characterized. Results of their interaction with bovine opsin are reported. The data have been analyzed in terms of the conformational properties of the retinal isomers and their steric compatibility with the binding site as defined by the two-dimensional map disclosed earlier. The need to expand the active zone and previously undetected restrictions in the third dimension are noted.
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D005136:Eye Proteins / Q000378:metabolism*; D007202:Indicators and Reagents; D007536:Isomerism; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D012168:Retinal Pigments / Q000378:metabolism*; D012172:Retinaldehyde / Q000031:analogs & derivatives / Q000138:chemical synthesis / Q000378:metabolism*; D012176:Retinoids / Q000378:metabolism*; D017299:Rod Opsins; D013329:Structure-Activity Relationship
D005136:Eye Proteins; D007202:Indicators and Reagents; D012168:Retinal Pigments; D012176:Retinoids; D017299:Rod Opsins; D012172:Retinaldehyde