Solution structure of the BHRF1 protein from Epstein-Barr virus, a homolog of human Bcl-2

J Mol Biol. 2003 Oct 3;332(5):1123-30. doi: 10.1016/j.jmb.2003.08.007.


The three-dimensional structure of BHRF1, the Bcl-2 homolog from Epstein-Barr virus (EBV), has been determined by NMR spectroscopy. Although the overall structure is similar to other Bcl-2 family members, there are important structural differences. Unlike some of the other Bcl-2 family members, BHRF1 does not contain the prominent hydrophobic groove that mediates binding to pro-apoptotic family members. In addition, in contrast to the anti-apoptotic Bcl-2 proteins, BHRF1 does not bind tightly to peptides derived from the pro-apoptotic proteins Bak, Bax, Bik, and Bad. The lack of an exposed, pre-formed binding groove in BHRF1 and the lack of significant binding to peptides derived from pro-apoptotic family members that bind to other anti-apoptotic family members, suggest that the mechanism of the BHRF1 anti-apoptotic activity does not parallel that of cellular Bcl-x(L) or Bcl-2.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Apoptosis
  • Binding Sites
  • Herpesvirus 4, Human / metabolism*
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Molecular Sequence Data
  • Peptides / chemistry
  • Protein Binding
  • Protein Conformation
  • Protein Structure, Secondary
  • Proto-Oncogene Proteins c-bcl-2 / chemistry*
  • Viral Proteins / chemistry*


  • BHRF1 protein, Human herpesvirus 4
  • Peptides
  • Proto-Oncogene Proteins c-bcl-2
  • Viral Proteins

Associated data

  • PDB/1Q59