Jin Tengchuan, Huang Mo, Jiang Jiansheng, Smith Patrick, Xiao Tsan Sam
Laboratory of structural immunology, CAS Key Laboratory of innate immunity and chronic diseases, CAS Center for Excellence in Molecular Cell Science, School of Life Sciences and Medical Center, University of Science and Technology of China, Hefei, Anhui, PRC.
Structural Immunobiology Unit, Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland, United States of America.
PLoS One. 2018 Jan 2;13(1):e0190547. doi: 10.1371/journal.pone.0190547. eCollection 2018.
NLRP12 is a NOD-like receptor that plays multiple roles in both inflammation and tumorigenesis. Despite the importance, little is known about its mechanism of action at the molecular level. Here, we report the crystal structure of NLRP12 PYD domain at 1.70 Å fused with an maltose-binding protein (MBP) tag. Interestingly, the PYD domain forms a dimeric configuration through a disulfide bond in the crystal. The possible biological significance is discussed in the context of ROS induced NF-κB activation.
NLRP12是一种核苷酸结合寡聚化结构域样受体，在炎症和肿瘤发生过程中发挥多种作用。尽管其重要性，但在分子水平上对其作用机制仍知之甚少。在此，我们报道了与麦芽糖结合蛋白（MBP）标签融合的NLRP12 PY结构域在1.70 Å分辨率下的晶体结构。有趣的是，在晶体中PY结构域通过二硫键形成二聚体结构。在活性氧诱导的核因子κB激活的背景下讨论了其可能的生物学意义。
