Download MendeleySolution Structure of the BHRF1 Protein From Epstein-Barr Virus, a Homolog of Human Bcl-2
Huang, Q., Petros, A.M., Virgin, H.W., Fesik, S.W., Olejniczak, E.T.(2003) J Mol Biol 332: 1123-1130
- PubMed: 14499614
- DOI: https://doi.org/10.1016/j.jmb.2003.08.007
- Primary Citation of Related Structures:
1Q59 - PubMed 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-x(L) or Bcl-2.
Organizational Affiliation:
Global Pharmaceutical Discovery Division, Abbott Laboratories, 100 Abbott Park Road, R46Y AP 10, Abbott Park, IL 0064-6098, USA.
