Activation and maturation of SARS-CoV main protease

Protein Cell. 2011 Apr;2(4):282-90. doi: 10.1007/s13238-011-1034-1. Epub 2011 Apr 28.

Abstract

The worldwide outbreak of the severe acute respiratory syndrome (SARS) in 2003 was due to the transmission of SARS coronavirus (SARS-CoV). The main protease (M(pro)) of SARS-CoV is essential for the viral life cycle, and is considered to be an attractive target of anti-SARS drug development. As a key enzyme for proteolytic processing of viral polyproteins to produce functional non-structure proteins, M(pro) is first auto-cleaved out of polyproteins. The monomeric form of M(pro) is enzymatically inactive, and it is activated through homo-dimerization which is strongly affected by extra residues to both ends of the mature enzyme. This review provides a summary of the related literatures on the study of the quaternary structure, activation, and self-maturation of M(pro) over the past years.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Coronavirus 3C Proteases
  • Crystallography, X-Ray
  • Cysteine Endopeptidases* / chemistry
  • Cysteine Endopeptidases* / metabolism
  • Enzyme Activation
  • Humans
  • Models, Molecular
  • Polyproteins / chemistry
  • Polyproteins / metabolism
  • Protein Multimerization
  • Protein Structure, Tertiary
  • SARS Virus / chemistry
  • SARS Virus / enzymology*
  • Severe Acute Respiratory Syndrome / virology*
  • Viral Proteins* / chemistry
  • Viral Proteins* / metabolism

Substances

  • Polyproteins
  • Viral Proteins
  • Cysteine Endopeptidases
  • Coronavirus 3C Proteases