Cell Reports volume 4, issue 2, P327-339 2013 DOI: 10.1016/j.celrep.2013.06.024 View full text
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Qian Yin, David P. Sester, Yuan Tian, Yu-Shan Hsiao, Alvin Lu, Jasmyn A. Cridland, Vitaliya Sagulenko, Sara J. Thygesen, Divaker Choubey, Veit Hornung, Thomas Walz, Katryn J. Stacey, Hao Wu

Abstract: SUMMARY Mouse p202 containing two HIN domains antagonizes AIM2 inflammasome signaling and potentially modifies lupus susceptibility. We found only HIN1 of p202 binds dsDNA, while HIN2 forms a homo-tetramer. Crystal structures of HIN1 revealed that dsDNA is bound on the opposite face to the site used in AIM2 and IFI16. The structure of HIN2 revealed a dimer of dimers, with the face analogous to the HIN1 dsDNA binding site being a dimerization interface. Electron microscopy imaging showed that HIN1 is flexibly …

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