Author: Sun, Di; Chen, Shun; Cheng, Anchun; Wang, Mingshu
Title: Roles of the Picornaviral 3C Proteinase in the Viral Life Cycle and Host Cells Document date: 2016_3_17
ID: 07nfb69o_6
Snippet: Picornavirus 3C pro s possesses a conserved Cys-His-Asp/Glu catalytic triad within the active site. This structure is similar to the Ser-His-Asp catalytic triad of serine proteases, except that third residue of the triad plays a less important catalytic role than in a serine protease. The catalytic residues in Figure 1 . The entire genome structure of poliovirus (PV) [9] . This RNA genome contains a 5 1 -nontranslated region (NTR), a large open r.....
Document: Picornavirus 3C pro s possesses a conserved Cys-His-Asp/Glu catalytic triad within the active site. This structure is similar to the Ser-His-Asp catalytic triad of serine proteases, except that third residue of the triad plays a less important catalytic role than in a serine protease. The catalytic residues in Figure 1 . The entire genome structure of poliovirus (PV) [9] . This RNA genome contains a 5 1 -nontranslated region (NTR), a large open reading frame, a 3 1 NTR and a poly (A) tail. A small viral-encoded protein, 3B (VPg), is linked to the 5 1 terminus of the RNA. The 5 1 NTR consists of a cloverleaf structure and a type II internal ribosome entry site (IRES) . The open reading frame encodes a single polyprotein comprising the structural protein P1 region and the non-structural protein P2 and P3 regions.
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