ArticleNature communications2020
Structure and dynamics of the active Gs-coupled human secretin receptor.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
36 citing papers in PubMed, 69 citations in OpenAlex.
- Potent and biased agonists of class B1 GPCRs from a heterochiral design strategy.Nature chemistry · 2026Article
- Structural basis of Neisseria meningitidis quinol dependent nitric oxide reductase activation by dimerization.Communications biology · 2026Article
- All roads lead to Rome: Emergence of Mechanistic Divergence Shapes Activation of Class B1 G-Protein Coupled Receptors.bioRxiv : the preprint server for biology · 2026Article
- Structural and mechanistic insights into dual activation of cagrilintide in amylin and calcitonin receptors.Acta pharmacologica Sinica · 2026Article
- The Concise Guide to PHARMACOLOGY 2025/26: G protein-coupled receptors.British journal of pharmacology · 2025Review
- 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
- A genome-wide association study identified 10 novel genomic loci associated with intrinsic capacity.The journals of gerontology. Series A, Biological sciences and medical sciences · 2025Article
- Mechanistic insights from the atomic-level quaternary structure of short-lived GPCR oligomers of the human secretin receptor in live cells.Communications biology · 2025Article
- A neuroimmune pathway drives bacterial infection.Science advances · 2025Article
- Hidden GPCR structural transitions addressed by multiple walker supervised molecular dynamics (mwSuMD).eLife · 2025Article
- GPCR Sense Communication Among Interaction Nematodes with Other Organisms.International journal of molecular sciences · 2025Review
- Mechanistic insights from the atomic-level quaternary structure of short-lived GPCR oligomers in live cells.Research square · 2024Article
- Impact of secretin receptor homo-dimerization on natural ligand binding.Nature communications · 2024Article
- Structural basis for lysophosphatidylserine recognition by GPR34.Nature communications · 2024Article
- Article
- Decrypting orphan GPCR drug discovery via multitask learning.Journal of cheminformatics · 2024Article
- Structure, function and drug discovery of GPCR signaling.Molecular biomedicine · 2023Review
- The Concise Guide to PHARMACOLOGY 2023/24: G protein-coupled receptors.British journal of pharmacology · 2023Article
- New Insights into the Structure and Function of Class B1 GPCRs.Endocrine reviews · 2023Article
- Molecular Mechanisms of PTH/PTHrP Class B GPCR Signaling and Pharmacological Implications.Endocrine reviews · 2023Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
15 authors at 6 institutions in 6 countries.
Funding
Abstract
The class B secretin GPCR (SecR) has broad physiological effects, with target potential for treatment of metabolic and cardiovascular disease. Molecular understanding of SecR binding and activation is important for its therapeutic exploitation. We combined cryo-electron microscopy, molecular dynamics, and biochemical cross-linking to determine a 2.3 Å structure, and interrogate dynamics, of secretin bound to the SecR:Gs complex. SecR exhibited a unique organization of its extracellular domain (ECD) relative to its 7-transmembrane (TM) core, forming more extended interactions than other family members. Numerous polar interactions formed between secretin and the receptor extracellular loops (ECLs) and TM helices. Cysteine-cross-linking, cryo-electron microscopy multivariate analysis and molecular dynamics simulations revealed that interactions between peptide and receptor were dynamic, and suggested a model for initial peptide engagement where early interactions between the far N-terminus of the peptide and SecR ECL2 likely occur following initial binding of the peptide C-terminus to the ECD.
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What OpenQuestion holds
Registered trials
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.