Unknown

Dataset Information

0

Evolutionary analysis of rhodopsin and cone pigments: connecting the three-dimensional structure with spectral tuning and signal transfer.


ABSTRACT: 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.

SUBMITTER: Teller DC 

PROVIDER: S-EPMC1468034 | biostudies-literature | 2003 Nov

REPOSITORIES: biostudies-literature

altmetric image

Publications

Evolutionary analysis of rhodopsin and cone pigments: connecting the three-dimensional structure with spectral tuning and signal transfer.

Teller David C DC   Stenkamp Ronald E RE   Palczewski Krzysztof K  

FEBS letters 20031101 1


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 t  ...[more]

Similar Datasets

| S-EPMC2492582 | biostudies-literature
| S-EPMC4536979 | biostudies-literature
| S-EPMC2491561 | biostudies-literature
| S-EPMC3064189 | biostudies-literature
| S-EPMC3021771 | biostudies-literature
| S-EPMC3223675 | biostudies-literature
| S-EPMC2810422 | biostudies-literature
| S-EPMC5798944 | biostudies-literature
| S-EPMC3497134 | biostudies-literature
| S-EPMC23167 | biostudies-literature