The opsins. Export

@article{citeulike:334858, abstract = {The photosensitive molecule rhodopsin and its relatives consist of a protein moiety - an opsin - and a non-protein moiety - the chromophore retinal. Opsins, which are G-protein-coupled receptors (GPCRs), are found in animals, and more than a thousand have been identified so far. Detailed molecular phylogenetic analyses show that the opsin family is divided into seven subfamilies, which correspond well to functional classifications within the family: the vertebrate visual (transducin-coupled) and non-visual opsin subfamily, the encephalopsin/tmt-opsin subfamily, the Gq-coupled opsin/melanopsin subfamily, the Go-coupled opsin subfamily, the neuropsin subfamily, the peropsin subfamily and the retinal photoisomerase subfamily. The subfamilies diversified before the deuterostomes (including vertebrates) split from the protostomes (most invertebrates), suggesting that a common animal ancestor had multiple opsin genes. Opsins have a seven-transmembrane structure similar to that of other GPCRs, but are distinguished by a lysine residue that is a retinal-binding site in the seventh helix. Accumulated evidence suggests that most opsins act as pigments that activate G proteins in a light-dependent manner in both visual and non-visual systems, whereas a few serve as retinal photoisomerases, generating the chromophore used by other opsins, and some opsins have unknown functions.}, address = {Department of Biophysics, Graduate School of Science, Kyoto University and Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Agency, Kyoto 606-8502, Japan. terakita@photo2.biophys.kyoto-u.ac.jp}, author = {Terakita, A.}, citeulike-article-id = {334858}, citeulike-linkout-0 = {http://dx.doi.org/10.1186/gb-2005-6-3-213}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/15774036}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=15774036}, doi = {10.1186/gb-2005-6-3-213}, issn = {1465-6914}, journal = {Genome Biol}, keywords = {26}, number = {3}, posted-at = {2008-03-12 15:13:03}, priority = {2}, title = {The opsins.}, url = {http://dx.doi.org/10.1186/gb-2005-6-3-213}, volume = {6}, year = {2005} }

TY - JOUR ID - citeulike:334858 L3 - citeulike-article-id:334858 N2 - The photosensitive molecule rhodopsin and its relatives consist of a protein moiety - an opsin - and a non-protein moiety - the chromophore retinal. Opsins, which are G-protein-coupled receptors (GPCRs), are found in animals, and more than a thousand have been identified so far. Detailed molecular phylogenetic analyses show that the opsin family is divided into seven subfamilies, which correspond well to functional classifications within the family: the vertebrate visual (transducin-coupled) and non-visual opsin subfamily, the encephalopsin/tmt-opsin subfamily, the Gq-coupled opsin/melanopsin subfamily, the Go-coupled opsin subfamily, the neuropsin subfamily, the peropsin subfamily and the retinal photoisomerase subfamily. The subfamilies diversified before the deuterostomes (including vertebrates) split from the protostomes (most invertebrates), suggesting that a common animal ancestor had multiple opsin genes. Opsins have a seven-transmembrane structure similar to that of other GPCRs, but are distinguished by a lysine residue that is a retinal-binding site in the seventh helix. Accumulated evidence suggests that most opsins act as pigments that activate G proteins in a light-dependent manner in both visual and non-visual systems, whereas a few serve as retinal photoisomerases, generating the chromophore used by other opsins, and some opsins have unknown functions. IS - 3 JF - Genome Biol SN - 1465-6914 AD - Department of Biophysics, Graduate School of Science, Kyoto University and Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Agency, Kyoto 606-8502, Japan. terakita@photo2.biophys.kyoto-u.ac.jp TI - The opsins. VL - 6 KW - 26 AU - Terakita, A PY - 2005/// UR - http://dx.doi.org/10.1186/gb-2005-6-3-213 ER -