Severe acute respiratory syndrome coronavirus 3C-like proteinase N terminus is indispensable for proteolytic activity but not for enzyme dimerization. Biochemical and thermodynamic investigation in conjunction with molecular dynamics simulations.

@article{Chen2005SevereAR,
  title={Severe acute respiratory syndrome coronavirus 3C-like proteinase N terminus is indispensable for proteolytic activity but not for enzyme dimerization. Biochemical and thermodynamic investigation in conjunction with molecular dynamics simulations.},
  author={Shuai X. Chen and Lili Chen and Jinzhi Tan and Jing Chen and Li Du and Tao Sun and Jianhua Shen and K. A. Chen and Hualiang Jiang and Xu Shen},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 1},
  pages={164-73}
}
Severe acute respiratory syndrome (SARS) coronavirus is a novel human coronavirus and is responsible for SARS infection. SARS coronavirus 3C-like proteinase (SARS 3CL(pro)) plays key roles in viral replication and transcription and is an attractive target for anti-SARS drug discovery. In this report, we quantitatively characterized the dimerization features of the full-length and N-terminal residues 1-7 deleted SARS 3CL(pro)s by using glutaraldehyde cross-linking SDS-PAGE, size-exclusion… CONTINUE READING

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