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Articles by Shuai Chen
Total Records ( 1 ) for Shuai Chen
  Shuai Chen , Tiancen Hu , Jian Zhang , Jing Chen , Kaixian Chen , Jianping Ding , Hualiang Jiang and Xu Shen
  SARS-CoV 3C-like protease (3CLpro) is an attractive target foranti-severe acute respiratory syndrome (SARS) drug discovery,and its dimerization has been extensively proved to be indispensablefor enzymatic activity. However, the reason why the dissociatedmonomer is inactive still remains unclear due to the absenceof the monomer structure. In this study, we showed that mutationof the dimer-interface residue Gly-11 to alanine entirely abolishedthe activity of SARS-CoV 3CLpro. Subsequently, we determinedthe crystal structure of this mutant and discovered a completecrystallographic dimer dissociation of SARS-CoV 3CLpro. Themutation might shorten the α-helix A` of domain I and cause amis-oriented N-terminal finger that could not correctly squeezeinto the pocket of another monomer during dimerization, thusdestabilizing the dimer structure. Several structural featuresessential for catalysis and substrate recognition are severelyimpaired in the G11A monomer. Moreover, domain III rotates dramaticallyagainst the chymotrypsin fold compared with the dimer, fromwhich we proposed a putative dimerization model for SARS-CoV3CLpro. As the first reported monomer structure for SARS-CoV3CLpro, the crystal structure of G11A mutant might provide insightinto the dimerization mechanism of the protease and supply directstructural evidence for the incompetence of the dissociatedmonomer.
 
 
 
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