| Literature DB >> 11333921 |
M R Hicks1, S Balesaria, C Medina-Palazon, M J Pandya, D N Woolfson, A J Sinclair.
Abstract
BZLF1 plays a key role in the induction of Epstein-Barr virus (EBV) replication. On the basis of limited sequence homology and mutagenesis experiments, BZLF1 has been described as a member of the bZip family of transcription factors, but this prospect has not been rigorously tested to date. Here, we present biophysical analysis of the multimerization domain of BZLF1, from three natural variants of EBV, and demonstrate for the first time that the region between amino acids 196 and 227 is sufficient to direct folding as a coiled-coil dimer in vitro.Entities:
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Year: 2001 PMID： 11333921 PMCID： PMC114945 DOI： 10.1128/JVI.75.11.5381-5384.2001
Source DB: PubMed Journal: J Virol ISSN： 0022-538X Impact factor: 5.103