ArticleNature communications2022
A distinctive ligand recognition mechanism by the human vasoactive intestinal polypeptide receptor 2.
Article in Nature communications, 2022. 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.
- Identification and characterization of vasoactive intestinal peptide receptor antagonists with high-affinity and potent anti-leukemia activity.The Journal of biological chemistry · 2026Article
- Structural basis of modified ligand selectivity from N-terminal PAC1R alternative splicing.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Exploring hypertension-linked diseases: a comprehensive review of innovative drug combinations with enhanced therapeutic potential.Naunyn-Schmiedeberg's archives of pharmacology · 2025Review
- Progresses in Questing for the Truth of Opioid-Related Constipation in Cancer Patients.Journal of cellular and molecular medicine · 2025Review
- Structure, function and drug discovery of GPCR signaling.Molecular biomedicine · 2023Review
- Molecular basis of signal transduction mediated by the human GIPR splice variants.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- The functional heterogeneity of PACAP: Stress, learning, and pathology.Neurobiology of learning and memory · 2023Review
- New Insights into the Structure and Function of Class B1 GPCRs.Endocrine reviews · 2023Article
- CHARMM-GUIJournal of chemical theory and computation · 2023Review
- Ligand recognition mechanism of the human relaxin family peptide receptor 4 (RXFP4).Nature communications · 2023Article
- Novel Fluorescently Labeled PACAP and VIP Highlight Differences between Peptide Internalization and Receptor Pharmacology.ACS pharmacology & translational science · 2023Article
- Article
- Targeting VIP and PACAP Receptor Signaling: New Insights into Designing Drugs for the PACAP Subfamily of Receptors.International journal of molecular sciences · 2022Review
- Article
Corrections and comments
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Authors and funding
16 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Class B1 of G protein-coupled receptors (GPCRs) comprises 15 members activated by physiologically important peptide hormones. Among them, vasoactive intestinal polypeptide receptor 2 (VIP2R) is expressed in the central and peripheral nervous systems and involved in a number of pathophysiological conditions, including pulmonary arterial hypertension, autoimmune and psychiatric disorders, in which it is thus a valuable drug target. Here, we report the cryo-electron microscopy structure of the human VIP2R bound to its endogenous ligand PACAP27 and the stimulatory G protein. Different from all reported peptide-bound class B1 GPCR structures, the N-terminal α-helix of VIP2R adopts a unique conformation that deeply inserts into a cleft between PACAP27 and the extracellular loop 1, thereby stabilizing the peptide-receptor interface. Its truncation or extension significantly decreased VIP2R-mediated cAMP accumulation. Our results provide additional information on peptide recognition and receptor activation among class B1 GPCRs and may facilitate the design of better therapeutics.
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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.