 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 5]](hv5242fig5mag.jpg)
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Figure 5
Binding of p202 to DNA prevents the formation of the AIM2/Aim2 inflammasome. (a) Crystal packing of the p202 HINa–dsDNA complex. Four asymmetric units indicated by black boxes are shown with their dsDNA chains forming a pseudo-duplex. (b) Schematic model of four adjacent p202 HINa molecules bound to dsDNA. (c) Schematic model of the p202 HINb tetramer observed in the crystal structure (PDB entry 4l5t ). (d) Schematic model of full-length p202 binding to DNA. The p202 HINb tetramer tethers four HINa domains together, which in turn bind to dsDNA simultaneously. (e) Crystal packing of the AIM2 HIN–dsDNA complex (PDB entry 3rn2 ). (f) Model of the negative regulation of AIM2/Aim2 signalling by p202. The HIN domain of AIM2/Aim2 binds to dsDNA, which leads to the oligomerization of its PYD domain. The p202 HINa domain competes with AIM2/Aim2 HIN for DNA binding, while the p202 HINb tetramer recruits the released AIM2/Aim2 HIN to two opposite ends. |
![[Figure 5]](hv5242fig5.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
