Crystal structure of the DNA-binding domain of the Epstein-Barr virus origin-binding protein EBNA1
Identifieur interne : 004093 ( Main/Exploration ); précédent : 004092; suivant : 004094Crystal structure of the DNA-binding domain of the Epstein-Barr virus origin-binding protein EBNA1
Auteurs : Alexey Bochkarev [Canada] ; Jean A. Barwell [Canada] ; Richard A. Pfuetzner [Canada] ; William Furey Jr. [États-Unis] ; Aled M. Edwards [Canada] ; Lori Frappier [Canada]Source :
- Cell [ 0092-8674 ] ; 1995.
English descriptors
- Teeft :
- Ambinder, Amino, Amino acid, Amino acids, Binding sites, Bovine papilloma virus, Bovine papillomavirus, Cooperative binding, Core domain, Crystal structure, Dimer, Dimerization, Domain, Dyad, Ebnai, Ebnal, Ebnal core domain, Ebnal dimer, Ebnal dimers, Electron density, Frappier, Hayward, Helix, Homology, Latent infection, Local dyad axis, Monomer, Nuclear antigen, Orip, Papillomavirus, Pcmb, Proline, Proline loop, Recognition element, Recognition helix, Replication, Residue, Side chains, Structural homology, Sugden, Viral, Virol.
Abstract
Abstract: The crystal structure of the DNA-binding and dimerization domains of the Epstein-Barr virus nuclear antigen 1 (EBNAI), 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 α helix whose N-terminus contacts the outer regions of the EBNA1 DNA recognition element.
Url:
DOI: 10.1016/0092-8674(95)90232-5
Affiliations:
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Barwell</name><affiliation wicri:level="1"><country>Canada</country><wicri:regionArea>Institute for Molecular Biology and Biotechnology Cancer Research Group Department of Pathology McMaster University Hamilton, Ontario</wicri:regionArea><wicri:noRegion>Ontario</wicri:noRegion></affiliation></author><author><name sortKey="Pfuetzner, Richard A" sort="Pfuetzner, Richard A" uniqKey="Pfuetzner R" first="Richard A." last="Pfuetzner">Richard A. Pfuetzner</name><affiliation wicri:level="1"><country>Canada</country><wicri:regionArea>Institute for Molecular Biology and Biotechnology Cancer Research Group Department of Pathology McMaster University Hamilton, Ontario</wicri:regionArea><wicri:noRegion>Ontario</wicri:noRegion></affiliation></author><author><name sortKey="Furey Jr, William" sort="Furey Jr, William" uniqKey="Furey Jr W" first="William" last="Furey Jr.">William Furey Jr.</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Pennsylvanie</region></placeName><wicri:cityArea>Veterans Administration Medical Center Biocrystallography Laboratory and Department of Crystallography University of Pittsburgh Pittsburgh</wicri:cityArea></affiliation></author><author><name sortKey="Edwards, Aled M" sort="Edwards, Aled M" uniqKey="Edwards A" first="Aled M." last="Edwards">Aled M. Edwards</name><affiliation wicri:level="1"><country>Canada</country><wicri:regionArea>Institute for Molecular Biology and Biotechnology Cancer Research Group Department of Pathology McMaster University Hamilton, Ontario</wicri:regionArea><wicri:noRegion>Ontario</wicri:noRegion></affiliation><affiliation></affiliation></author><author><name sortKey="Frappier, Lori" sort="Frappier, Lori" uniqKey="Frappier L" first="Lori" last="Frappier">Lori Frappier</name><affiliation wicri:level="1"><country>Canada</country><wicri:regionArea>Institute for Molecular Biology and Biotechnology Cancer Research Group Department of Pathology McMaster University Hamilton, Ontario</wicri:regionArea><wicri:noRegion>Ontario</wicri:noRegion></affiliation><affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Cell</title><title level="j" type="abbrev">CELL</title><idno type="ISSN">0092-8674</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1995">1995</date><biblScope unit="volume">83</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="39">39</biblScope><biblScope unit="page" to="46">46</biblScope></imprint><idno type="ISSN">0092-8674</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0092-8674</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Ambinder</term><term>Amino</term><term>Amino acid</term><term>Amino acids</term><term>Binding sites</term><term>Bovine papilloma virus</term><term>Bovine papillomavirus</term><term>Cooperative binding</term><term>Core domain</term><term>Crystal structure</term><term>Dimer</term><term>Dimerization</term><term>Domain</term><term>Dyad</term><term>Ebnai</term><term>Ebnal</term><term>Ebnal core domain</term><term>Ebnal dimer</term><term>Ebnal dimers</term><term>Electron density</term><term>Frappier</term><term>Hayward</term><term>Helix</term><term>Homology</term><term>Latent infection</term><term>Local dyad axis</term><term>Monomer</term><term>Nuclear antigen</term><term>Orip</term><term>Papillomavirus</term><term>Pcmb</term><term>Proline</term><term>Proline loop</term><term>Recognition element</term><term>Recognition helix</term><term>Replication</term><term>Residue</term><term>Side chains</term><term>Structural homology</term><term>Sugden</term><term>Viral</term><term>Virol</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The crystal structure of the DNA-binding and dimerization domains of the Epstein-Barr virus nuclear antigen 1 (EBNAI), 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 α helix whose N-terminus contacts the outer regions of the EBNA1 DNA recognition element.</div></front></TEI><affiliations><list><country><li>Canada</li><li>États-Unis</li></country><region><li>Pennsylvanie</li></region></list><tree><country name="Canada"><noRegion><name sortKey="Bochkarev, Alexey" sort="Bochkarev, Alexey" uniqKey="Bochkarev A" first="Alexey" last="Bochkarev">Alexey Bochkarev</name></noRegion><name sortKey="Barwell, Jean A" sort="Barwell, Jean A" uniqKey="Barwell J" first="Jean A." last="Barwell">Jean A. Barwell</name><name sortKey="Edwards, Aled M" sort="Edwards, Aled M" uniqKey="Edwards A" first="Aled M." last="Edwards">Aled M. Edwards</name><name sortKey="Frappier, Lori" sort="Frappier, Lori" uniqKey="Frappier L" first="Lori" last="Frappier">Lori Frappier</name><name sortKey="Pfuetzner, Richard A" sort="Pfuetzner, Richard A" uniqKey="Pfuetzner R" first="Richard A." last="Pfuetzner">Richard A. Pfuetzner</name></country><country name="États-Unis"><region name="Pennsylvanie"><name sortKey="Furey Jr, William" sort="Furey Jr, William" uniqKey="Furey Jr W" first="William" last="Furey Jr.">William Furey Jr.</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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