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  • Title: Crystal structure of the DNA-binding domain of the Epstein-Barr virus origin-binding protein EBNA 1.
    Author: Bochkarev A, Barwell JA, Pfuetzner RA, Furey W, Edwards AM, Frappier L.
    Journal: Cell; 1995 Oct 06; 83(1):39-46. PubMed ID: 7553871.
    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.
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