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Structural basis of peptide recognition and activation of endothelin receptors
Open accessPreprint — published as 10.1038/s41467-023-36998-9
Abstract
Endothelin system comprises three endogenous 21-amino-acid peptide ligands endothelin-1, -2, and -3 (ET-1/2/3), and two G protein-coupled receptor (GPCR) subtypes—endothelin receptor A (ET A R) and B (ET B R). Since ET-1, the first endothelin, was identified in 1988 as one of the most potent endothelial cell-derived vasoconstrictor peptides with long-lasting actions, the endothelin system has attracted extensive attention due to its critical role in vasoregulation and close relevance in cardiovascular-related diseases. Here we present three cryo-electron microscopy structures of ET A R and ET B R bound to ET-1 and ET B R bound to the selective peptide IRL1620. These structures reveal a highly conserved recognition mode of ET-1 and characterize the ligand selectivity by ETRs. They also present several conformation features of the active ETRs, thus revealing a specific activation mechanism. Together, these findings deepen our understanding of endothelin system regulation and offer an opportunity to design selective drugs targeting specific ETR subtypes.
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Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
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Metadata
- Authors
- Ji, Y., Duan, J., Yuan, Q., He, X., Yang, G., Zhu, S., Wu, K., Hu, W., Gao, T., Cheng, X., Jiang, H., Xu, H. E., & Jiang, Y.
- Affiliations
- Chinese Academy of Sciences (CN)
- Xiamen University (CN)
- Macau University of Science and Technology (MO)
- ShanghaiTech University (CN)
- Corresponding author
- Duan, Jia
- Xu, H. Eric
- Jiang, Yi
- Venue
- Nature Communications
- Publisher
- openRxiv
- Published
- 2023-01-18
- Volume
- 14
- Issue
- 1
- Pages
- 1268-1268
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC9992518
- OpenAlex
- W4323355656
- Cited by
- 31
- References
- 1
- Citations by year
- 2026: 5 · 2025: 12 · 2024: 12 · 2023: 2
- FWCI
- 2.75
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Nature Communications (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Ministry of Science and Technology of the People's Republic of China (2018YFA0507002)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- endothelin receptors, endothelin-1, ETA receptor, endothelin B receptor, G protein-coupled receptors, peptide recognition, receptor activation mechanism, ligand selectivity, receptor conformation, vascular regulation, cryo-EM structure
- MeSH terms
- Amino Acids, Cardiovascular Diseases, Humans, Peptides, Endothelin-1, Cryoelectron Microscopy, Receptor, Endothelin A
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