Opioid receptors are G-protein-coupled receptors (GPCRs) part of cell signaling paths of direct interest The potentially low pH at tissue targeted by opioid drugs in pain management could impact drug binding to the opioid receptor, because opioid drugs typically have a protonated amino group that contributes to receptor binding, and the functioning of GPCRs may involve protonation change. In this review, we discuss the relationship between structure, function, and dynamics of opioid receptors

The bioactive lysophospholipid sphingosine-1-phosphate (S1P) acts via five different subtypes of S1P receptors Several S1PR therapeutic drugs have been developed to treat these diseases; however, they lack receptor In this article, we describe a 2.2 Å resolution room temperature crystal structure of the human S1P5 receptor The structure demonstrates a unique ligand-binding mode, involving an allosteric sub-pocket, which clarifies the receptor subtype selectivity and provides a template for structure-based drug design.

influence predominantly arises via engagement with the principal two G-protein-coupled cannabinoid receptors Earlier publications have indicated that expression of CB1 receptor mRNA and protein has been recognized The part played by CB1 receptor activation or inhibition with respect to these functions and relevant This can be deduced from the qRT-PCR assays; triggering CB1 receptors amplifies both NR4A1 and NR4A3 The impact of ACEA is inhibited by the selective CB1 receptor antagonist, rimonabant.

< GPCR News < GPCRs in Oncology and Immunology Stable Binding of Full-Length Chemerin is Driven by Negative 1 (CMKLR1), a member of the family of G protein-coupled receptors (GPCR). Using receptor chimera of G protein-coupled receptor 1 (GPR1) and CMKLR1, we were able to identify the residues of this interaction and its relevance for stable full-length chemerin binding. Tags double mutant cycle analysis , protein expression , protein-protein interaction , receptor binding

Professor Pfleger has developed extensive expertise in profiling receptor binding and function at the globally-recognized expertise in bioluminescence resonance energy transfer (BRET) technology, including his patented Receptor-Heteromer Investigation Technology (Receptor-HIT) for studying heteromers.

doctoral dissertation was the first large-scale study of structure-activity relationships for adenosine receptors postdoc with John W Daly at NIH and Solomon Snyder at Johns Hopkins, he developed the first adenosine receptor binding assay. He then joined WL/PD, where his lab demonstrated the existence of two subtypes of the adenosine A2 receptor In 1988, he joined Lilly as a receptor biologist in charge of a high-throughput screening lab.