Download MendeleyCrystal structure of the DNA-binding domain of the Epstein-Barr virus origin-binding protein EBNA 1.
Bochkarev, A., Barwell, J.A., Pfuetzner, R.A., Furey Jr., W., Edwards, A.M., Frappier, L.(1995) Cell 83: 39-46
- PubMed: 7553871
- DOI: https://doi.org/10.1016/0092-8674(95)90232-5
- Primary Citation of Related Structures:
1VHI - PubMed Abstract:
The crystal structure of the DNA-binding and dimerization domains of the Epstein-Barr virus nuclear antigen 1 (EBNA1), which binds to and activates DNA replication from the latent origin of replication in Epstein-Barr virus, was solved at 2.5 A resolution. EBNA1 appears to bind DNA via two independent regions termed the core and the flanking DNA-binding domains. The core DNA-binding domain, which comprises both the dimerization domain and a helix predicted to bind the inner portion of the EBNA1 DNA recognition element, was remarkably similar to the structure of the papillomavirus E2 protein, despite a complete lack of sequence conservation. The flanking DNA-binding domain, only a portion of which is contained in the current structure, consists in part of an alpha helix whose N-terminus contacts the outer regions of the EBNA1 DNA recognition element.
Organizational Affiliation:
Department of Pathology, McMaster University, Hamilton, Ontario, Canada.
