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

Qiulong Huang, Andrew M. Petros, Herbert W. Virgin, Stephen W. Fesik, Edward T. Olejniczak

Research output: Contribution to journalArticlepeer-review

76 Scopus citations

Abstract

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-xL or Bcl-2.

Original languageEnglish
Pages (from-to)1123-1130
Number of pages8
JournalJournal of Molecular Biology
Volume332
Issue number5
DOIs
StatePublished - Oct 3 2003

Keywords

  • BHRF1
  • Bcl-2
  • Epstein-Barr virus
  • NMR spectroscopy
  • Structure determination

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