Publication Abstract from PubMed
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.
Crystal structure of the DNA-binding domain of the Epstein-Barr virus origin-binding protein EBNA 1.,Bochkarev A, Barwell JA, Pfuetzner RA, Furey W Jr, Edwards AM, Frappier L Cell. 1995 Oct 6;83(1):39-46. PMID:7553871[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
