Proteases universally recognize beta strands in their active sites

Chem Rev. 2005 Mar;105(3):973-99. doi: 10.1021/cr040669e.
No abstract available

Publication types

  • Review

MeSH terms

  • Animals
  • Aspartic Acid Endopeptidases / chemistry
  • Aspartic Acid Endopeptidases / metabolism
  • Binding Sites
  • Cysteine Endopeptidases / chemistry
  • Cysteine Endopeptidases / metabolism
  • Humans
  • Metalloproteases / chemistry
  • Metalloproteases / metabolism
  • Peptide Hydrolases / chemistry
  • Peptide Hydrolases / metabolism*
  • Protease Inhibitors / chemistry*
  • Protease Inhibitors / metabolism
  • Protein Structure, Secondary*
  • Serine Endopeptidases / chemistry
  • Serine Endopeptidases / metabolism
  • Structure-Activity Relationship
  • Substrate Specificity

Substances

  • Protease Inhibitors
  • Metalloproteases
  • Peptide Hydrolases
  • Serine Endopeptidases
  • Cysteine Endopeptidases
  • Aspartic Acid Endopeptidases