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The normal transport of substances in the nucleus and cytoplasm is necessary for the maintenance of normal physiological functions of cells, and in the case of viral infection, it is also crucial
Deng Hongyu's research group and Gao Pu's research group from the Institute of Biophysics of the Chinese Academy of Sciences collaborated in 2020 to analyze the ternary complex structure of the herpes virus MHV-68 ORF10 protein and the host mRNA transport complex Rae1-Nup98, and revealed the molecular mechanism of ORF10 selectively inhibiting mRNA nuclear transport (PNAS, 2020).
Sarbecovirus (including SARS-CoV-2, SARS-CoV and other viruses) not only has a large number of mutations in the S protein, breaking through the protective effect of neutralizing antibodies and vaccines, but also has the ability to
The researchers analyzed the crystal structure of the two complexes formed by the auxiliary protein ORF6 C-terminal fragment (CTT) of SARS-CoV and SARS-CoV and the nuclear pore complex component Rae1-Nup98, respectively, and then used various techniques such as biochemical, biophysical and cell function experiments to reveal the molecular mechanism
Next, the researchers performed systematic mutations on ORF6, and through Co-IP experiments, expression determination of GFP reporter genes, nucleoplasmic distribution determination of GFP-mRNA, interferon reporting system, and immunofluorescence, the key amino acid sites of ORF6 and Rae1-Nup98 interaction were clarified, revealing that the affinity of ORF6 CTT and Rae1-Nup98 was positively correlated with the function of ORF6 inhibiting mRNA nucleation and STAT molecules entering the nucleus.
The crystal structure of the composites SARS-CoV-2/SARS-CoV ORF6 and Rae1-Nup98 and their inhibition of nucleoplasmic transport
Cui Sheng and Deng Hongyu are the co-corresponding authors of the paper, Gao Xiaopan, associate researcher of Cui Sheng's research group, Tian Huabin, assistant researcher of Deng Hongyu's research group, and Zhu Kaixiang, postdoctoral fellow of Cui Sheng's research group, are the co-first authors
Article link: https://rdcu.
(Contributed by: Deng Hongyu Research Group)
