Induced structure of a helical switch as a mechanism to regulate enzymatic activity

Nat Struct Mol Biol. 2005 Nov;12(11):1019-20. doi: 10.1038/nsmb1006.


Herpesviruses encode a protease that is activated by homodimerization at high enzyme concentrations during lytic replication. The homodimer contains two active sites, which are distal from the dimer interface. Assignment of backbone NMR resonances and engineering of a redox switch show that two helices position a loop containing catalytic residues within each active site.

Publication types

  • Comparative Study
  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Catalysis
  • Dimerization
  • Herpesvirus 8, Human / enzymology*
  • Models, Molecular*
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Conformation
  • Protein Engineering
  • Serine Endopeptidases / chemistry*
  • Serine Endopeptidases / metabolism*
  • Structure-Activity Relationship


  • Serine Endopeptidases
  • human herpesvirus 8 protease