کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
6138463 | 1594223 | 2016 | 11 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Structural basis for the dimerization and substrate recognition specificity of porcine epidemic diarrhea virus 3C-like protease
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
ایمنی شناسی و میکروب شناسی
ویروس شناسی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Structural basis for the dimerization and substrate recognition specificity of porcine epidemic diarrhea virus 3C-like protease Structural basis for the dimerization and substrate recognition specificity of porcine epidemic diarrhea virus 3C-like protease](/preview/png/6138463.png)
چکیده انگلیسی
Porcine epidemic diarrhea virus (PEDV), a member of the genus Alphacoronavirus, has caused significant damage to the Asian and American pork industries. Coronavirus 3C-like protease (3CLpro), which is involved in the processing of viral polyproteins for viral replication, is an appealing antiviral drug target. Here, we present the crystal structures of PEDV 3CLpro and a molecular complex between an inactive PEDV 3CLpro variant C144A bound to a peptide substrate. Structural characterization, mutagenesis and biochemical analysis reveal the substrate-binding pockets and the residues that comprise the active site of PEDV 3CLpro. The dimerization of PEDV 3CLpro is similar to that of other Alphacoronavirus 3CLpros but has several differences from that of SARS-CoV 3CLpro from the genus Betacoronavirus. Furthermore, the non-conserved motifs in the pockets cause different cleavage of substrate between PEDV and SARS-CoV 3CLpros, which may provide new insights into the recognition of substrates by 3CLpros in various coronavirus genera.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Virology - Volume 494, July 2016, Pages 225-235
Journal: Virology - Volume 494, July 2016, Pages 225-235
نویسندگان
Gang Ye, Feng Deng, Zhou Shen, Rui Luo, Ling Zhao, Shaobo Xiao, Zhen F. Fu, Guiqing Peng,