Design of peptide inhibitors that bind the bZIP domain of Epstein-Barr virus protein BZLF1.

ABSTRACT: Designing proteins or peptides that bind native protein targets can aid the development of novel reagents and/or therapeutics. Rational design also tests our understanding of the principles underlying protein recognition. This article describes several strategies used to design peptides that bind to the basic region leucine zipper (bZIP) domain of the viral transcription factor BZLF1, which is encoded by the Epstein-Barr virus. BZLF1 regulates the transition of the Epstein-Barr virus from a latent state to a lytic state. It shares some properties in common with the more studied human bZIP transcription factors, but also includes novel structural elements that pose interesting challenges to inhibitor design. In designing peptides that bind to BZLF1 by forming a coiled-coil structure, we con

SUBMITTER: Chen TS 

PROVIDER: S-EPMC3087387 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature