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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Crystal structure of the DNA-binding domain of the Epstein-Barr virus origin-binding protein EBNA 1.

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.[1]

References

  1. Crystal 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, W., Edwards, A.M., Frappier, L. Cell (1995) [Pubmed]
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