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4LEY

Structure of mouse cGAS bound to 18 bp DNA

Summary for 4LEY
Entry DOI10.2210/pdb4ley/pdb
Related4LEV 4LEw 4LEz
DescriptorCyclic GMP-AMP synthase, 18 bp dsDNA, ZINC ION, ... (4 entities in total)
Functional Keywordsntase, dna sensor, transferase-dna complex, transferase/dna
Biological sourceMus musculus (mouse)
More
Cellular locationCytoplasm, cytosol: Q8C6L5
Total number of polymer chains12
Total formula weight216317.12
Authors
Li, P. (deposition date: 2013-06-26, release date: 2013-12-25, Last modification date: 2024-04-03)
Primary citationLi, X.,Shu, C.,Yi, G.,Chaton, C.T.,Shelton, C.L.,Diao, J.,Zuo, X.,Kao, C.C.,Herr, A.B.,Li, P.
Cyclic GMP-AMP Synthase Is Activated by Double-Stranded DNA-Induced Oligomerization.
Immunity, 39:1019-1031, 2013
Cited by
PubMed Abstract: Cyclic GMP-AMP synthase (cGAS) is a cytosolic DNA sensor mediating innate antimicrobial immunity. It catalyzes the synthesis of a noncanonical cyclic dinucleotide, 2',5' cGAMP, that binds to STING and mediates the activation of TBK1 and IRF-3. Activated IRF-3 translocates to the nucleus and initiates the transcription of the IFN-β gene. The structure of mouse cGAS bound to an 18 bp dsDNA revealed that cGAS interacts with dsDNA through two binding sites, forming a 2:2 complex. Enzyme assays and IFN-β reporter assays of cGAS mutants demonstrated that interactions at both DNA binding sites are essential for cGAS activation. Mutagenesis and DNA binding studies showed that the two sites bind dsDNA cooperatively and that site B plays a critical role in DNA binding. The structure of mouse cGAS bound to dsDNA and 2',5' cGAMP provided insight into the catalytic mechanism of cGAS. These results demonstrated that cGAS is activated by dsDNA-induced oligomerization.
PubMed: 24332030
DOI: 10.1016/j.immuni.2013.10.019
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

238268

数据于2025-07-02公开中

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