Conformational Flexibility of a Short Loop near the Active Site of the SARS-3CLpro is Essential to Maintain Catalytic Activity.

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作者： Chunmei,Li ^[1] ; Xin,Teng ^[2] ; Yifei,Qi ^[1] ; Bo,Tang ^[2] ; Hailing,Shi ^[1] ; Xiaomin,Ma ^[1] ; Luhua,Lai ^[2]

作者单位： BNLMS, State Key Laboratory for Structural Chemistry of Unstable and Stable Species, College of Chemistry and Molecular Engineering, Peking University, Beijing, 100871, China. ^[1] Center for Quantitative Biology, Peking University, Beijing, 100871, China. ^[2]

主题词氨基酸特征结构(Amino Acid Motifs);催化作用(Catalysis);催化域(Catalytic Domain);半胱氨酸内肽酶类(Cysteine Endopeptidases);酶激活(Enzyme Activation);亲水和疏水相互作用(Hydrophobic and Hydrophilic Interactions);模型, 分子(Models, Molecular);分子动力学模拟(Molecular Dynamics Simulation);突变(Mutation);蛋白质构象(Protein Conformation);蛋白质多聚化(Protein Multimerization);蛋白质亚单位(Protein Subunits);病毒蛋白质类(Viral Proteins)

DOI 10.1038/srep20918

PMID 26879383

发布时间 2020-12-09

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Conformational Flexibility of a Short Loop near the Active Site of the SARS-3CLpro is Essential to Maintain Catalytic Activity.

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Conformational Flexibility of a Short Loop near the Active Site of the SARS-3CLpro is Essential to Maintain Catalytic Activity.

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