Author: Chuck, Chi-Pang; Chow, Hak-Fun; Wan, David Chi-Cheong; Wong, Kam-Bo
Title: Profiling of Substrate Specificities of 3C-Like Proteases from Group 1, 2a, 2b, and 3 Coronaviruses Document date: 2011_11_2
ID: 0vu7bobr_13
Snippet: The protease activities correlate negatively with side chain volume, and positively with the hydrophobicity of substituting residues at P4 position ( Figure 2 ). The correlations with hydrophobicity were more evident (with correlation coefficients .0.89) when only small residues (Ala, Asn, Asp, Cys, Gly, Ser, and Thr) with side chain volumes ,70 Ã… 3 ( Figure 3 ) were included in the analysis. This result suggests that as long as the side chain c.....
Document: The protease activities correlate negatively with side chain volume, and positively with the hydrophobicity of substituting residues at P4 position ( Figure 2 ). The correlations with hydrophobicity were more evident (with correlation coefficients .0.89) when only small residues (Ala, Asn, Asp, Cys, Gly, Ser, and Thr) with side chain volumes ,70 Ã… 3 ( Figure 3 ) were included in the analysis. This result suggests that as long as the side chain can fit into the P4 binding pocket, the protease activity is directly proportional to the hydrophobicity of the substituting residues. On the other hand, charged residues like Lys, Arg, His, Asp and Glu were not cleavable, presumably due to the unfavorable burial of charges in the hydrophobic P4 pocket.
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