ArticleCommunications biology2025
Structure of the complex of C1q-like 3 protein with adhesion-GPCR BAI3.
Article in Communications biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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The trial behind it
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Who cites it
8 citing papers in PubMed.
- Brain-Wide Mapping and Synaptic Localization of C1QL3 Using a Novel Epitope-Tagged Knock-In Mouse.The Journal of comparative neurology · 2026Article
- Tethered agonist- and GAIN domain-independent signaling of an adhesion GPCR.Science advances · 2026Article
- The therapeutic potential of orphan adhesion G-protein-coupled receptors.Nature reviews. Drug discovery · 2026Review
- Therapeutic targeting of adhesion GPCRs: a status update and future potential.Expert opinion on drug discovery · 2026Review
- Adhesion G protein-coupled receptors.Pharmacological reviews · 2026Review
- BAI adhesion-GPCRs perform distinct functions in neural development differentially controlled by RTN4R and C1ql ligands.Nature communications · 2025Article
- Structural basis of calcium-dependent C1ql1/BAI3 assemblies in synaptic connectivity.Nature communications · 2025Article
- Adhesion G-Protein Coupled Receptors in Neurological and Psychiatric Disorders.Journal of psychiatry and brain science · 2025Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
The adhesion-GPCR Brain-specific Angiogenesis Inhibitor-3 (BAI3) plays a crucial role in organizing synapses in the brain. However, how BAI3 engages one of its ligands, the C1q-like proteins (C1qls), remains largely unexplored. Here, we present the single-particle cryo-electron microscopy (cryo-EM) structure of the C1ql3-BAI3 complex at 2.8 Å resolution. The structure reveals a hexameric configuration, where C1ql3 forms a central homotrimer that effectively captures three BAI3 molecules. These BAI3 molecules fit snugly into the grooves between the trimeric C1q domains of the C1qls, employing calcium ion (Ca
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Registered trials
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