1vhi

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1vhi, resolution 2.5Å

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EPSTEIN BARR VIRUS NUCLEAR ANTIGEN-1 DNA-BINDING DOMAIN, RESIDUES 470-607

Overview

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.

About this Structure

1VHI is a Single protein structure of sequence from Human herpesvirus 4. Full crystallographic information is available from OCA.

Reference

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

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