ArticleNature communications2024
The structural basis for 2'-5'/3'-5'-cGAMP synthesis by cGAS.
Article in Nature communications, 2024. 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.
- Inhibition by ATP regulates the activity of a CBASS anti-phage nucleotide cyclase.The Biochemical journal · 2026Article
- Protein•DNA mesh assembly drives dsDNA-specific and duplex length-dependent activation of cGAS.bioRxiv : the preprint server for biology · 2026Article
- Extracellular cGAMP in health and disease.Molecular biomedicine · 2026Review
- The Enzymatic Mechanism of OAS: How Metal Ions and Quantum Effects Help Activate Innate Immunity.ACS omega · 2026Article
- Dimerization-dependent gel-like condensation with dsDNA underpins the activation of human cGAS.Cell reports · 2026Article
- cGAS-STING Pathway in Gastrointestinal Malignancies: Mechanistic Insights and Translational Therapeutic Opportunities.Journal of gastrointestinal cancer · 2026Review
- cGAS-STING pathway in innate immunity and its cell-specific role in kidney diseases.Frontiers in immunology · 2026Review
- Structural biology at the National Synchrotron Light Source II.Journal of synchrotron radiation · 2025Article
- cGAS, an innate dsDNA sensor with multifaceted functions.Cell insight · 2025Review
- PCK1 inhibits cGAS-STING activation by consumption of GTP to promote tumor immune evasion.The Journal of experimental medicine · 2025Article
- cGAS-STING: mechanisms and therapeutic opportunities.Science China. Life sciences · 2025Review
- Structural insight into the cGAS active site explains differences between therapeutically relevant species.Communications chemistry · 2025Article
- The adjuvant effect of manganese on tuberculosis subunit vaccine Bfrb-GrpE.NPJ vaccines · 2024Article
- Inhibitors of the Cyclic GMP-AMP Synthase (cGAS) as Potential Treatment for Autoimmune and Inflammatory Diseases.ACS medicinal chemistry letters · 2024Article
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Authors and funding
3 authors.
Funding
Abstract
cGAS activates innate immune responses against cytosolic double-stranded DNA. Here, by determining crystal structures of cGAS at various reaction stages, we report a unifying catalytic mechanism. apo-cGAS assumes an array of inactive conformations and binds NTPs nonproductively. Dimerization-coupled double-stranded DNA-binding then affixes the active site into a rigid lock for productive metal•substrate binding. A web-like network of protein•NTP, intra-NTP, and inter-NTP interactions ensures the stepwise synthesis of 2'-5'/3'-5'-linked cGAMP while discriminating against noncognate NTPs and off-pathway intermediates. One divalent metal is sufficient for productive substrate binding, and capturing the second divalent metal is tightly coupled to nucleotide and linkage specificities, a process which manganese is preferred over magnesium by 100-fold. Additionally, we elucidate how mouse cGAS achieves more stringent NTP and linkage specificities than human cGAS. Together, our results reveal that an adaptable, yet precise lock-and-key-like mechanism underpins cGAS catalysis.
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