ArticleNature communications2025
Inactive structures of the vasopressin V2 receptor reveal distinct binding modes for Tolvaptan and Mambaquaretin toxin.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Universal pipeline for high-resolution GPCR structure determination.Nature structural & molecular biology · 2026Article
- Protein Engineering-Enabled Cryo-EM Investigation of Small GTPases.Journal of molecular biology · 2026Article
- SAR-Guided Scaffold Innovation of Selective VACS medicinal chemistry letters · 2026Article
- Molecular basis of antagonism of the dimeric human arginine vasopressin receptor 1A.Nature communications · 2026Article
- Structural insights into antagonist recognition by the vasopressin V2 receptor.Nature communications · 2025Article
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Authors and funding
12 authors.
Funding
Abstract
Inhibitors of the arginine-vasopressin (AVP) V2 receptor (V2R) are key therapeutic compounds for treating hyponatremia or polycystic kidney diseases. Rational drug design based on experimental G protein-coupled receptor structures is a powerful avenue to develop better drugs. So far, the lack of inhibitor-bound V2R structures has impaired this strategy. Here we describe the cryo-electron microscopy structures of the V2R in complex with two selective inverse agonists, the non-peptide Tolvaptan (TVP) and the green mamba snake Mambaquaretin toxin (MQ1). Both ligands bind into the orthosteric binding site but with substantial differences. TVP binds deeper than MQ1, and directly contacts the toggle switch residue W284
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