Sakmar T.P., Fahmy K.
Properties and photoactivity of rhodopsin mutants
Isr. J. Chem. 1995;35(3-4):325-337.
A variety of spectroscopic and biochemical studies of recombinant site-directed mutants of rhodopsin and related visual pigments have been carried out. These studies have elucidated key structural elements common to visual pigments, such as a conserved disulfide bond. In addition, systematic analysis of the chromophore-binding pocket in rhodopsin and cone pigments has led to an improved understanding of the mechanism of the opsin-shift, and of particular molecular determinants underlying color vision in humans. Identification of conformational changes which occur upon rhodopsin photoactivation has been of particular recent concern. Assignment of these molecular alterations to specific regions in the receptor has been attempted by studying native opsin regenerated with synthetic retinal analogues or recombinant opsins regenerated with 11-cis-retinal. Individual molecular groups that undergo structural alterations during photoactivation have been identified. Analysis of particular mutant pigments in which specific groups are locked into their respective 'on' or 'off' states has provided a framework to identify determinants of the active conformation as well as the minimal number of intramolecular transitions required to switch between inactive and active conformations. A simple model for the active state of rhodopsin can be compared to structural models of its ground state to localize chromophore-protein interactions that may be important in the photoactivation mechanism.