ArticleStructure (London, England : 1993)2020
Crystal Structure of β-Arrestin 2 in Complex with CXCR7 Phosphopeptide.
Article in Structure (London, England : 1993), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
What it found
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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
37 citing papers in PubMed, 61 citations in OpenAlex.
- Arrestins as programmable integrators of GPCR signaling: structural microstates, spatiotemporal logic, and therapeutic control.Cell discovery · 2026Review
- Subtype-dependent arrestin engagement of the metabotropic glutamate receptors.Nature communications · 2026Article
- Inhibition of constitutive activity of the atypical chemokine receptor 3 by the small-molecule inverse agonist VUF16840.Molecular pharmacology · 2025Article
- Molecular mechanism of β-arrestin 2 interaction with phosphorylated intracellular loop 3 of dopamine receptor D2.Communications biology · 2025Article
- An arginine switch drives the stepwise activation of β-arrestin by CXCR7.PLoS biology · 2025Article
- Article
- Conformational dynamics of the active state of β-arrestin 1.bioRxiv : the preprint server for biology · 2025Article
- Lipids modulate the dynamics of GPCR:β-arrestin interaction.Nature communications · 2025Article
- Biased Signaling Agonists Promote Distinct Phosphorylation and Conformational States of the Dopamine D3 Receptor.International journal of molecular sciences · 2024Article
- Phosphorylation patterns in the AT1R C-terminal tail specify distinct downstream signaling pathways.Science signaling · 2024Article
- Control of G protein-coupled receptor function via membrane-interacting intrinsically disordered C-terminal domains.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Arrestins: A Small Family of Multi-Functional Proteins.International journal of molecular sciences · 2024Review
- Control of G protein-coupled receptor function via membrane-interacting intrinsically disordered C-terminal domains.bioRxiv : the preprint server for biology · 2024Article
- Structure, function and drug discovery of GPCR signaling.Molecular biomedicine · 2023Review
- Molecular insights into intrinsic transducer-coupling bias in the CXCR4-CXCR7 system.Nature communications · 2023Article
- ACKR3-arrestin2/3 complexes reveal molecular consequences of GRK-dependent barcoding.bioRxiv : the preprint server for biology · 2023Article
- GPCR targeting of E3 ubiquitin ligase MDM2 by inactive β-arrestin.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Structural snapshots uncover a key phosphorylation motif in GPCRs driving β-arrestin activation.Molecular cell · 2023Article
- Article
- ClickArr: a novel, high-throughput assay for evaluating β-arrestin isoform recruitment.Frontiers in pharmacology · 2023Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
β-Arrestins (βarrs) critically regulate G-protein-coupled receptor (GPCR) signaling and trafficking. βarrs have two isoforms, βarr1 and βarr2. Receptor phosphorylation is a key determinant for the binding of βarrs, and understanding the intricate details of receptor-βarr interaction is the next frontier in GPCR structural biology. The high-resolution structure of active βarr1 in complex with a phosphopeptide derived from GPCR has been revealed, but that of βarr2 remains elusive. Here, we present a 2.3-Å crystal structure of βarr2 in complex with a phosphopeptide (C7pp) derived from the carboxyl terminus of CXCR7. The structural analysis of C7pp-bound βarr2 reveals key differences from the previously determined active conformation of βarr1. One of the key differences is that C7pp-bound βarr2 shows a relatively small inter-domain rotation. Antibody-fragment-based conformational sensor and hydrogen/deuterium exchange experiments further corroborated the structural features of βarr2 and suggested that βarr2 adopts a range of inter-domain rotations.
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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.