A G protein-coupled receptor at work: the rhodopsin model. Export

@article{citeulike:5980275, abstract = {G protein-coupled receptors (GPCRs) are ubiquitous signal transducers in cell membranes, as well as important drug targets. Interaction with extracellular agonists turns the seven transmembrane helix (7TM) scaffold of a GPCR into a catalyst for GDP and GTP exchange in heterotrimeric Galphabetagamma proteins. Activation of the model GPCR, rhodopsin, is triggered by photoisomerization of its retinal ligand. From the augmentation of biochemical and biophysical studies by recent high-resolution 3D structures, its activation intermediates can now be interpreted as the stepwise engagement of protein domains. Rearrangement of TM5-TM6 opens a crevice at the cytoplasmic side of the receptor into which the C terminus of the Galpha subunit can bind. The Galpha C-terminal helix is used as a transmission rod to the nucleotide binding site. The mechanism relies on dynamic interactions between conserved residues and could therefore be common to other GPCRs.}, author = {Hofmann, Klaus Peter P. and Scheerer, Patrick and Hildebrand, Peter W. and Choe, Hui-Woog W. and Park, Jung Hee H. and Heck, Martin and Ernst, Oliver P.}, citeulike-article-id = {5980275}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.tibs.2009.07.005}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/19836958}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=19836958}, day = {15}, doi = {10.1016/j.tibs.2009.07.005}, issn = {0968-0004}, journal = {Trends in biochemical sciences}, keywords = {activation, gpcr, review, rhodopsin}, month = {November}, number = {11}, pages = {540--552}, posted-at = {2009-11-09 14:10:06}, priority = {2}, title = {A G protein-coupled receptor at work: the rhodopsin model.}, url = {http://dx.doi.org/10.1016/j.tibs.2009.07.005}, volume = {34}, year = {2009} }

TY - JOUR ID - citeulike:5980275 L3 - citeulike-article-id:5980275 N2 - G protein-coupled receptors (GPCRs) are ubiquitous signal transducers in cell membranes, as well as important drug targets. Interaction with extracellular agonists turns the seven transmembrane helix (7TM) scaffold of a GPCR into a catalyst for GDP and GTP exchange in heterotrimeric Galphabetagamma proteins. Activation of the model GPCR, rhodopsin, is triggered by photoisomerization of its retinal ligand. From the augmentation of biochemical and biophysical studies by recent high-resolution 3D structures, its activation intermediates can now be interpreted as the stepwise engagement of protein domains. Rearrangement of TM5-TM6 opens a crevice at the cytoplasmic side of the receptor into which the C terminus of the Galpha subunit can bind. The Galpha C-terminal helix is used as a transmission rod to the nucleotide binding site. The mechanism relies on dynamic interactions between conserved residues and could therefore be common to other GPCRs. IS - 11 JF - Trends in biochemical sciences SN - 0968-0004 EP - 552 TI - A G protein-coupled receptor at work: the rhodopsin model. VL - 34 SP - 540 KW - activation KW - gpcr KW - review KW - rhodopsin AU - Hofmann, Klaus Peter AU - Scheerer, Patrick AU - Hildebrand, Peter AU - Choe, Hui-Woog AU - Park, Jung Hee AU - Heck, Martin AU - Ernst, Oliver PY - 2009/11/15/ UR - http://dx.doi.org/10.1016/j.tibs.2009.07.005 ER -