image: An illustration of computer modelled structures of complexes formed between RXFP3 and relaxin-3 or relaxin-3 B-chain stapled peptides. (A) shows relaxin-3 binding to RXFP3, while (B to D) show different stapled relaxin-3 B-chain peptides binding to RXFP3. Binding of the various peptides at the top of the receptor outside the cell, results in different configurations at the bottom of the receptor inside the cells. It is proposed that these different configurations differentially trigger the RXFP3 signalling pathways inside the cell.
Credit: Credit: NUS Yong Loo Lin School of Medicine and University of Colombo, Sri Lanka
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Professor Gavin Dawe,
Head, Department of Pharmacology, Yong Loo Lin School of Medicine, National University of Singapore (NUS Medicine)
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Gavin Dawe教授
新加坡国立大学杨潞龄医学院 药理学系主管 |
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Dr Tharindunee Jayakody,
PhD alumna, Department of Pharmacology, Yong Loo Lin School of Medicine, National University of Singapore (NUS Medicine)
Lecturer, Department of Chemistry, Faculty of Science, University of Colombo, Sri Lanka |
Tharindunee Jayakody博士
新加坡国立大学杨潞龄医学院 药理学系博士校友
Lecturer, Department of Chemistry, Faculty of Science, University of Colombo, Sri Lanka |
Journal
Science Signaling
Method of Research
Experimental study
Subject of Research
Not applicable
Article Title
Mechanisms of biased agonism by Gαi/o-biased stapled peptide agonists of the relaxin-3 receptor
Article Publication Date
13-Feb-2024