%0 Journal Article %1 Hoffmann2008a %A Hoffmann, C. %A Zurn, A. %A Bunemann, M. %A Lohse, M. J. %D 2008 %J Br J Pharmacol %K Agents/pharmacology Animals Chelating Conformation Drug/chemistry/drug Energy Fluorescence G-Protein-Coupled/*chemistry/drug Humans M3/chemistry/drug Muscarinic Protein Resonance Rhodopsin/chemistry/drug Transfer beta-2/chemistry/drug effects Receptor Adrenergic %P S358-66 %T Conformational changes in G-protein-coupled receptors-the quest for functionally selective conformations is open %U http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=18059316 %V 153 Suppl 1 %X The G-protein-coupled receptors (GPCRs) represent one the largest families of drug targets. Upon agonist binding a receptor undergoes conformational rearrangements that lead to a novel protein conformation which in turn can interact with effector proteins. During the last decade significant progress has been made to prove that different conformational changes occur. Today it is mostly accepted that individual ligands can induce different receptor conformations. However, the nature or molecular identity of the different conformations is still ill-known. Knowledge of the potential functionally selective conformations will help to develop drugs that select specific conformations of a given GPCR which couple to specific signalling pathways and may, ultimately, lead to reduced side effects. In this review we will summarize recent progress in biophysical approaches that have led to the current understanding of conformational changes that occur during GPCR activation.

@article{Hoffmann2008a, abstract = {The G-protein-coupled receptors (GPCRs) represent one the largest families of drug targets. Upon agonist binding a receptor undergoes conformational rearrangements that lead to a novel protein conformation which in turn can interact with effector proteins. During the last decade significant progress has been made to prove that different conformational changes occur. Today it is mostly accepted that individual ligands can induce different receptor conformations. However, the nature or molecular identity of the different conformations is still ill-known. Knowledge of the potential functionally selective conformations will help to develop drugs that select specific conformations of a given GPCR which couple to specific signalling pathways and may, ultimately, lead to reduced side effects. In this review we will summarize recent progress in biophysical approaches that have led to the current understanding of conformational changes that occur during GPCR activation.}, added-at = {2010-12-14T18:12:02.000+0100}, author = {Hoffmann, C. and Zurn, A. and Bunemann, M. and Lohse, M. J.}, biburl = {https://www.bibsonomy.org/bibtex/2d96044af10383effdd2b95a362cad955/pharmawuerz}, endnotereftype = {Journal Article}, interhash = {ba2d8ccb798a7a716c785fa8cfd84743}, intrahash = {d96044af10383effdd2b95a362cad955}, issn = {0007-1188 (Print) 0007-1188 (Linking)}, journal = {Br J Pharmacol}, keywords = {Agents/pharmacology Animals Chelating Conformation Drug/chemistry/drug Energy Fluorescence G-Protein-Coupled/*chemistry/drug Humans M3/chemistry/drug Muscarinic Protein Resonance Rhodopsin/chemistry/drug Transfer beta-2/chemistry/drug effects Receptor Adrenergic}, month = Mar, note = {Hoffmann, C Zurn, A Bunemann, M Lohse, M J Research Support, Non-U.S. Gov't Review England British journal of pharmacology Br J Pharmacol. 2008 Mar;153 Suppl 1:S358-66. Epub 2007 Dec 3.}, pages = {S358-66}, shorttitle = {Conformational changes in G-protein-coupled receptors-the quest for functionally selective conformations is open}, timestamp = {2010-12-14T18:22:40.000+0100}, title = {Conformational changes in G-protein-coupled receptors-the quest for functionally selective conformations is open}, url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=18059316}, volume = {153 Suppl 1}, year = 2008 }