Crystallization and preliminary X-ray characterization of Epstein-Barr virus BHRF1 in complex with a benzoylurea peptidomimetic
Sofia Caria, Srishti Chugh, Nhu Duong, Guillaume Lessene, Marc Kvansakul
Acta Crystallographica Section F - Structural Biology and Crystallization Communications | INT UNION CRYSTALLOGRAPHY | Published : 2012
BHRF1 is a pro-survival Bcl-2 homologue encoded by Epstein-Barr virus (EBV) that plays a key role in preventing premature host cell death during viral infection and may contribute to the development of malignancies associated with chronic EBV infections. The anti-apoptotic action of BHRF1 is based on its ability to sequester pro-apoptotic Bcl-2 family proteins, in particular Bim and Bak. These interactions have been previously studied in three dimensions by determining crystal structures of BHRF1 in complex with both Bim and Bak BH3 domains. Screening of a library of peptidomimetic compounds based on the benzoylurea scaffold that mimics critical Bim BH3 domain side chains against BHRF1 led t..View full abstract
Awarded by NHMRC
We would like to thank the staff at the CSIRO Collaborative Crystallization Centre for the set-up of crystal screens and the staff of the MX team at the Australian Synchrotron for assistance with X-ray diffraction data collection. This work was funded by the NHMRC (fellowship to MK, project grant No. 637336).