Opsin shift in an aldolase antibody.
An antibody-retinal assembly that mimics the opsin shift (OS) of the naturally occurring visual pigments is reported. Both experiments and calculations show that the aldolase antibody 33F12 covalently binds all-trans retinal via a protonated Schiff base with a lysine residue. This chromophore, which exhibits a remarkable opsin red shift (140 nm), represents a useful model system for studying the factors that contribute to the OS.
Grynszpan
F
F
The Scripps Research Institute, Department of Molecular Biology and the Skaggs Institute for Chemical Biology, La Jolla, CA 92037, USA.
Keinan
E
E
D000906:Antibodies / Q000737:chemistry* / Q000276:immunology; D001666:Binding Sites, Antibody; D005634:Fructose-Bisphosphate Aldolase / Q000276:immunology*; D008958:Models, Molecular; D012172:Retinaldehyde / Q000276:immunology; D017299:Rod Opsins / Q000737:chemistry*; D012545:Schiff Bases; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013056:Spectrophotometry, Ultraviolet
D000906:Antibodies; D017299:Rod Opsins; D012545:Schiff Bases; D005634:Fructose-Bisphosphate Aldolase; D012172:Retinaldehyde