ArticleProceedings of the National Academy of Sciences of the United States of America2023
Cryo-EM structure of the human chemerin receptor 1-Gi protein complex bound to the C-terminal nonapeptide of chemerin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 20 citations in OpenAlex.
- Agonist-specific FPR1 conformational change prevents receptor recycling and promotes targeted protein degradation.Acta pharmaceutica Sinica. B · 2026Article
- Decoding chemerin proteolytic processing and isoform signaling across disease contexts.iScience · 2026Review
- Multiscale Computational Dissection of CCRL2-Mediated Chemerin Presentation.Journal of chemical information and modeling · 2025Article
- Chemerin and the Gut: From Inflammation to Cancer.Biomedicines · 2025Review
- Single-cell stemness analysis highlights Midkine-LRP1 pathway and identifies new bladder cancer subtypes.Cancer cell international · 2025Article
- Structural insights into GPCR signaling activated by peptide ligands: from molecular mechanism to therapeutic application.Experimental & molecular medicine · 2025Review
- Discovery ofActa pharmaceutica Sinica. B · 2025Article
- Similar Binding Mode of a 5-Sulfonylthiouracil Derivative Antagonist at Chemerin Receptors CMKLR1 and GPR1.Journal of medicinal chemistry · 2025Article
- Structural insights into the distinct ligand recognition and signaling of the chemerin receptors CMKLR1 and GPR1.Protein & cell · 2025Article
- The biological function and research progress of the adipokine chemerin in tumorigenesis and development.Journal of Cancer · 2025Review
- Structural basis for full-length chemerin recognition and signaling through chemerin receptor 1.Communications biology · 2024Article
- Review
- Structure of G protein-coupled receptor GPR1 bound to full-length chemerin adipokine reveals a chemokine-like reverse binding mode.PLoS biology · 2024Article
- Structural basis of G protein-Coupled receptor CMKLR1 activation and signaling induced by a chemerin-derived agonist.PLoS biology · 2023Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Chemerin is a processed protein that acts on G protein-coupled receptors (GPCRs) for its chemotactic and adipokine activities. The biologically active chemerin (chemerin 21-157) results from proteolytic cleavage of prochemerin and uses its C-terminal peptide containing the sequence YFPGQFAFS for receptor activation. Here we report a high-resolution cryo-electron microscopy (cryo-EM) structure of human chemerin receptor 1 (CMKLR1) bound to the C-terminal nonapeptide of chemokine (C9) in complex with Gi proteins. C9 inserts its C terminus into the binding pocket and is stabilized through hydrophobic interactions involving its Y1, F2, F6, and F8, as well as polar interactions between G4, S9, and several amino acids lining the binding pocket of CMKLR1. Microsecond scale molecular dynamics simulations support a balanced force distribution across the whole ligand-receptor interface that enhances thermodynamic stability of the captured binding pose of C9. The C9 interaction with CMKLR1 is drastically different from chemokine recognition by chemokine receptors, which follow a two-site two-step model. In contrast, C9 takes an "S"-shaped pose in the binding pocket of CMKLR1 much like angiotensin II in the AT1 receptor. Our mutagenesis and functional analyses confirmed the cryo-EM structure and key residues in the binding pocket for these interactions. Our findings provide a structural basis for chemerin recognition by CMKLR1 for the established chemotactic and adipokine activities.
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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.