ArticleNature communications2016
The complex binding mode of the peptide hormone H2 relaxin to its receptor RXFP1.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 53 citations in OpenAlex.
- Divergent activation of the RXFP1 relaxin receptor by protein and small molecule agonists.bioRxiv : the preprint server for biology · 2026Article
- The diverse influences of relaxin-like peptide family on tumor progression: Potential opportunities and emerging challenges.Heliyon · 2024Review
- The relaxin receptor RXFP1 signals through a mechanism of autoinhibition.Nature chemical biology · 2023Article
- Development of Novel High-Affinity Antagonists for the Relaxin Family Peptide Receptor 1.ACS pharmacology & translational science · 2023Article
- A Lipidated Single-B-Chain Derivative of Relaxin Exhibits Improved In Vitro Serum Stability without Altering Activity.International journal of molecular sciences · 2023Article
- Characterization of a new potent and long-lasting single chain peptide agonist of RXFP1 in cells and in vivo translational models.Scientific reports · 2022Article
- Expression and Characterization of Relaxin Family Peptide Receptor 1 Variants.Frontiers in pharmacology · 2021Article
- Structural Complexity and Plasticity of Signaling Regulation at the Melanocortin-4 Receptor.International journal of molecular sciences · 2020Review
- The relaxin family peptide receptor 1 (RXFP1): An emerging player in human health and disease.Molecular genetics & genomic medicine · 2020Review
- Fluorescent ligands: Bringing light to emerging GPCR paradigms.British journal of pharmacology · 2020Review
- Relaxin reverses maladaptive remodeling of the aged heart through Wnt-signaling.Scientific reports · 2019Article
- Familial bilateral cryptorchidism is caused by recessive variants inJournal of medical genetics · 2019Article
- Using the novel HiBiT tag to label cell surface relaxin receptors for BRET proximity analysis.Pharmacology research & perspectives · 2019Article
- Multi-Component Mechanism of H2 Relaxin Binding to RXFP1 through NanoBRET Kinetic Analysis.iScience · 2019Article
- Measuring translational diffusion ofEuropean biophysics journal : EBJ · 2018Article
- Tadpole-like Conformations of Huntingtin Exon 1 Are Characterized by Conformational Heterogeneity that Persists regardless of Polyglutamine Length.Journal of molecular biology · 2018Article
- In search of a small molecule agonist of the relaxin receptor RXFP1 for the treatment of liver fibrosis.Scientific reports · 2017Article
- Development of a selective agonist for relaxin family peptide receptor 3.Scientific reports · 2017Article
- Distinct activation modes of the Relaxin Family Peptide Receptor 2 in response to insulin-like peptide 3 and relaxin.Scientific reports · 2017Article
- ML290 is a biased allosteric agonist at the relaxin receptor RXFP1.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
H2 relaxin activates the relaxin family peptide receptor-1 (RXFP1), a class A G-protein coupled receptor, by a poorly understood mechanism. The ectodomain of RXFP1 comprises an N-terminal LDLa module, essential for activation, tethered to a leucine-rich repeat (LRR) domain by a 32-residue linker. H2 relaxin is hypothesized to bind with high affinity to the LRR domain enabling the LDLa module to bind and activate the transmembrane domain of RXFP1. Here we define a relaxin-binding site on the LDLa-LRR linker, essential for the high affinity of H2 relaxin for the ectodomain of RXFP1, and show that residues within the LDLa-LRR linker are critical for receptor activation. We propose H2 relaxin binds and stabilizes a helical conformation of the LDLa-LRR linker that positions residues of both the linker and the LDLa module to bind the transmembrane domain and activate RXFP1.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.