PT  - JOURNAL ARTICLE
AU  - Dezhong Yin
AU  - Shai Gavi
AU  - Hsien-yu Wang
AU  - Craig C. Malbon
TI  - Probing Receptor Structure/Function with Chimeric G-Protein-Coupled Receptors
AID  - 10.1124/mol.65.6.1323
DP  - 2004 Jun 01
TA  - Molecular Pharmacology
PG  - 1323--1332
VI  - 65
IP  - 6
4099  - http://molpharm.aspetjournals.org/content/65/6/1323.short
4100  - http://molpharm.aspetjournals.org/content/65/6/1323.full
SO  - Mol Pharmacol2004 Jun 01; 65
AB  - Owing its name to an image borrowed from Greek mythology, a chimera is seen to represent a new entity created as a composite from existing creatures or, in this case, molecules. Making use of various combinations of three basic domains of the receptors (i.e., exofacial, transmembrane, and cytoplasmic segments) that couple agonist binding into activation of effectors through heterotrimeric G-proteins, molecular pharmacology has probed the basic organization, structure/function relationships of this superfamily of heptahelical receptors. Chimeric G-protein-coupled receptors obviate the need for a particular agonist ligand when the ligand is resistant to purification or, in the case of orphan receptors, is not known. Chimeric receptors created from distant members of the heptahelical receptors enable new strategies in understanding how these receptors transduce agonist binding into receptor activation and may be able to offer insights into the evolution of G-protein-coupled receptors from yeast to humans.