Selected article for: "1B domain and crystal structure"
Author: Hao, Wei; Wojdyla, Justyna Aleksandra; Zhao, Rong; Han, Ruiyun; Das, Rajat; Zlatev, Ivan; Manoharan, Muthiah; Wang, Meitian; Cui, Sheng
Title: Crystal structure of Middle East respiratory syndrome coronavirus helicase
  • Document date: 2017_6_26
    • ID: 0vxhgjss_28
    Snippet: Recently, Zhang et al found that mutation A335V of MHV nsp13 led to attenuation of virus growth in cells and resulted in~30 fold reduced viral titer in the livers of infected mice [33] . Residue A335 of MHV nsp13 is highly conserved among CoVs nsp13 (S2 Fig). Based on the crystal structure of MERS-CoV nsp13, A335 (corresponding to A336 of MERS-CoV nsp13) is located on the β17-β18-loop, a loop interacts with the 1B domain as well as participates.....
    Document: Recently, Zhang et al found that mutation A335V of MHV nsp13 led to attenuation of virus growth in cells and resulted in~30 fold reduced viral titer in the livers of infected mice [33] . Residue A335 of MHV nsp13 is highly conserved among CoVs nsp13 (S2 Fig). Based on the crystal structure of MERS-CoV nsp13, A335 (corresponding to A336 of MERS-CoV nsp13) is located on the β17-β18-loop, a loop interacts with the 1B domain as well as participates in the formation of RNA binding channel. Because A335 is highly exposed to the surface of nsp13, Valine replacement could increase hydrophobicity of this region. Therefore, A335V mutation may impair the function of nsp13 by destabilizing the local structure critical to RNA binding or promoting aggregation of the protein.

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