Prediction of quaternary assembly of SARS coronavirus peplomer

Biochem Biophys Res Commun. 2004 Dec 24;325(4):1210-4. doi: 10.1016/j.bbrc.2004.10.156.

Abstract

The tertiary structures of the S1 and S2 domains of the spike protein of the coronavirus which is responsible of the severe acute respiratory syndrome (SARS) have been recently predicted. Here a molecular assembly of SARS coronavirus peplomer which accounts for the available functional data is suggested. The interaction between S1 and S2 appears to be stabilised by a large hydrophobic network of aromatic side chains present in both domains. This feature results to be common to all coronaviruses, suggesting potential targeting for drugs preventing coronavirus-related infections.

Publication types

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

MeSH terms

  • Amino Acid Substitution
  • Binding Sites
  • Computer Simulation
  • Membrane Glycoproteins / analysis
  • Membrane Glycoproteins / chemistry*
  • Models, Chemical*
  • Models, Molecular*
  • Protein Binding
  • Protein Conformation
  • Protein Structure, Quaternary
  • Protein Structure, Tertiary
  • Sequence Analysis, Protein / methods*
  • Spike Glycoprotein, Coronavirus
  • Structure-Activity Relationship
  • Viral Envelope Proteins / analysis
  • Viral Envelope Proteins / chemistry*

Substances

  • Membrane Glycoproteins
  • Spike Glycoprotein, Coronavirus
  • Viral Envelope Proteins
  • spike glycoprotein, SARS-CoV