| http://purl.uniprot.org/citations/30684458 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/30684458 | http://www.w3.org/2000/01/rdf-schema#comment | "Relaxin family peptides perform a variety of biological functions by activating four G protein-coupled receptors, namely relaxin family peptide receptor 1-4 (RXFP1-4). We recently disclosed electrostatic interactions of the homologous RXFP3 and RXFP4 with some agonists based on activation complementation. However, this activation assay-based approach cannot be applied to antagonists that do not activate receptors. Herein, we propose a general approach suitable for both agonists and antagonists based on our newly-developed NanoBiT-based binding assay. We first validated the binding assay-based approach using the agonist relaxin-3, then applied it to the chimeric antagonist R3(ΔB23-27)R/I5. Three positively charged B-chain Arg residues of the agonist and antagonist were respectively replaced by a negatively charged Glu residue; meanwhile, the negatively charged Glu and Asp residue in the essential WxxExxxD motif of both receptors were respectively replaced by a positively charged Arg residue. Based on binding complementation of mutant ligands towards mutant receptors, we deduced possible electrostatic interactions of the agonist and antagonist with both RXFP3 and RXFP4: their B-chain C-terminal Arg residue interacts with the deeply buried Glu residue in the WxxExxxD motif of both receptors, and one or two of their B-chain central Arg residues interact with the shallowly buried Asp residue in the WxxExxxD motif of both receptors. Our present work shed new light on the interaction mechanism of RXFP3 and RXFP4 with agonists and antagonists, and also provided a novel approach for interaction studies of some plasma membrane receptors with their ligands."xsd:string |
| http://purl.uniprot.org/citations/30684458 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbamem.2019.01.010"xsd:string |
| http://purl.uniprot.org/citations/30684458 | http://purl.uniprot.org/core/author | "Wang J.H."xsd:string |
| http://purl.uniprot.org/citations/30684458 | http://purl.uniprot.org/core/author | "Xu Z.G."xsd:string |
| http://purl.uniprot.org/citations/30684458 | http://purl.uniprot.org/core/author | "Liu Y.L."xsd:string |
| http://purl.uniprot.org/citations/30684458 | http://purl.uniprot.org/core/author | "Nie W.H."xsd:string |
| http://purl.uniprot.org/citations/30684458 | http://purl.uniprot.org/core/author | "Shao X.X."xsd:string |
| http://purl.uniprot.org/citations/30684458 | http://purl.uniprot.org/core/author | "Li H.Z."xsd:string |
| http://purl.uniprot.org/citations/30684458 | http://purl.uniprot.org/core/author | "Guo Z.Y."xsd:string |
| http://purl.uniprot.org/citations/30684458 | http://purl.uniprot.org/core/author | "Hu M.J."xsd:string |
| http://purl.uniprot.org/citations/30684458 | http://purl.uniprot.org/core/date | "2019"xsd:gYear |
| http://purl.uniprot.org/citations/30684458 | http://purl.uniprot.org/core/name | "Biochim Biophys Acta Biomembr"xsd:string |
| http://purl.uniprot.org/citations/30684458 | http://purl.uniprot.org/core/pages | "776-786"xsd:string |
| http://purl.uniprot.org/citations/30684458 | http://purl.uniprot.org/core/title | "Exploring electrostatic interactions of relaxin family peptide receptor 3 and 4 with ligands using a NanoBiT-based binding assay."xsd:string |
| http://purl.uniprot.org/citations/30684458 | http://purl.uniprot.org/core/volume | "1861"xsd:string |
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