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Evolutionary analysis of rhodopsin and cone pigments: connecting the three‐dimensional structure with spectral tuning and signal transfer
Author(s) -
Teller David C.,
Stenkamp Ronald E.,
Palczewski Krzysztof
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01152-9
Subject(s) - rhodopsin , opsin , visual phototransduction , biophysics , chromophore , biology , photopigment , chemistry , biochemistry , retinal , organic chemistry
Extensive sequence data and structural sampling of expressed proteins from different species lead to the idea that entire molecules or specific domain folds belong to large superfamilies of proteins. A subset of G protein‐coupled receptors, one of the largest families involved in cellular signaling, rod and cone opsins are involved in phototransduction in photoreceptor cells. Here, the evolutionary analysis of opsin sequences and structures predicts key residues involved in the transmission of the signal from the binding site of the chromophore to the cytoplasmic surface and residues that are involved in the spectral tuning of opsins to short wavelengths of light.