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

Huang Q, Petros AM, Virgin HW, Fesik SW, Olejniczak ET
J Mol Biol. 2003 332 (5): 1123-30

PMID: 14499614 · 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.

MeSH Terms (13)

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

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