Abstract
Cyclic GMP-AMP synthase (cGAS) is a cytosolic DNA sensor that detects pathogenic, foreign, or damaged DNA and is a key player in host defense, cancer, and autoimmune disorders. Upon DNA binding and dimerization, cGAS becomes activated and produces the second messenger cyclic GMP-AMP (cGAMP), which triggers the innate immune response. To prevent cGAS activation when it encounters self-DNA, cGAS binds to and is inhibited by nucleosomes, the fundamental repeating unit of chromatin. in order to investigate the molecular details of this cGAS-nucleosome interaction, we determined the 3.3 Å cryo-EM structure of cGAS bound to the nucleosome core particle.
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