2. Academic Validation
  3. Allosteric modulation of the G protein-coupled US28 receptor of human cytomegalovirus: are the small-weight inverse agonist of US28 'camouflaged' agonists?

Allosteric modulation of the G protein-coupled US28 receptor of human cytomegalovirus: are the small-weight inverse agonist of US28 'camouflaged' agonists?

  • Bioorg Med Chem Lett. 2014 Aug 15;24(16):3744-7. doi: 10.1016/j.bmcl.2014.06.082.
Nuska Tschammer 1
Affiliations

Affiliation

  • 1 Department of Chemistry and Pharmacy, Division of Medicinal Chemistry, Emil Fischer Center, Friedrich Alexander University, Schuhstr. 19, D-91052 Erlangen, Germany. Electronic address: [email protected].
PMID: 25052428 DOI: 10.1016/j.bmcl.2014.06.082
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.

Keywords

Allosteric modulation; Efficacy switch; G protein-coupled receptor; Human cytomegalovirus; Inverse agonism; US28.

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