title: Allosteric modulation of the G protein-coupled US28 receptor of human cytomegalovirus: are the small-weight inverse agonist of US28 'camouflaged' agonists?
abstract: The highly constitutively active G protein-coupled receptor US28 of human cytomegalovirus (HCMV) is thought to camouflage agonism by mediating constitutive endocytosis. With the use of the US28Δ300 mutant, which is largely devoid of constitutive internalization, I have demonstrated that the coupling of the receptor to its downstream signaling partners is responsible for the inverse agonism to agonism efficacy switch in some small-weight ligands of US28.
authors: Department of Chemistry and Pharmacy, Division of Medicinal Chemistry, Emil Fischer Center, Friedrich Alexander University, Schuhstr. 19, D-91052 Erlangen, Germany. Electronic address: nuska.tschammer@fau.de.
authors: Nuska
authors: N
authors: Tschammer
mesh_terms: D000494:Allosteric Regulation / Q000187:drug effects; D018946:Chemokine CCL5 / Q000737:chemistry / Q000494:pharmacology*; D054428:Chemokine CX3CL1 / Q000737:chemistry / Q000494:pharmacology*; D004305:Dose-Response Relationship, Drug; D057809:HEK293 Cells; D006801:Humans; D008024:Ligands; D015394:Molecular Structure; D008970:Molecular Weight; D010880:Piperidines / Q000737:chemistry / Q000494:pharmacology*; D019707:Receptors, Chemokine / Q000819:agonists* / Q000235:genetics; D013329:Structure-Activity Relationship; D014764:Viral Proteins / Q000819:agonists* / Q000235:genetics
chemical_list: D018946:Chemokine CCL5; D054428:Chemokine CX3CL1; D008024:Ligands; D010880:Piperidines; D019707:Receptors, Chemokine; C411191:US28 receptor, Cytomegalovirus; C473351:VUF 2274; D014764:Viral Proteins
keywords: Allosteric modulation; Efficacy switch; G protein-coupled receptor; Human cytomegalovirus; Inverse agonism; US28