Crystal structure of the DNA-binding domain of the Epstein-Barr virus origin-binding protein EBNA1
Identifieur interne : 002094 ( Istex/Corpus ); précédent : 002093; suivant : 002095Crystal structure of the DNA-binding domain of the Epstein-Barr virus origin-binding protein EBNA1
Auteurs : Alexey Bochkarev ; Jean A. Barwell ; Richard A. Pfuetzner ; William Furey Jr. ; Aled M. Edwards ; Lori FrappierSource :
- 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
Links to Exploration step
ISTEX:4CF9DDD9CD8B61733A7B04D6B8B0523FDDAB2E09Le document en format XML
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Edwards</name><affiliation><mods:affiliation>Institute for Molecular Biology and Biotechnology Cancer Research Group Department of Pathology McMaster University Hamilton, Ontario, Canada L8N 3Z5</mods:affiliation></affiliation><affiliation><mods:affiliation>‡ These authors contributed equally to this work.</mods:affiliation></affiliation></author><author><name sortKey="Frappier, Lori" sort="Frappier, Lori" uniqKey="Frappier L" first="Lori" last="Frappier">Lori Frappier</name><affiliation><mods:affiliation>Institute for Molecular Biology and Biotechnology Cancer Research Group Department of Pathology McMaster University Hamilton, Ontario, Canada L8N 3Z5</mods:affiliation></affiliation><affiliation><mods:affiliation>‡ These authors contributed equally to this work.</mods: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><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>ebnal</json:string><json:string>helix</json:string><json:string>ebnai</json:string><json:string>dimer</json:string><json:string>replication</json:string><json:string>viral</json:string><json:string>frappier</json:string><json:string>dimerization</json:string><json:string>virol</json:string><json:string>core domain</json:string><json:string>homology</json:string><json:string>recognition helix</json:string><json:string>sugden</json:string><json:string>amino acids</json:string><json:string>ambinder</json:string><json:string>dyad</json:string><json:string>proline</json:string><json:string>papillomavirus</json:string><json:string>pcmb</json:string><json:string>orip</json:string><json:string>amino</json:string><json:string>ebnal core domain</json:string><json:string>proline loop</json:string><json:string>monomer</json:string><json:string>hayward</json:string><json:string>amino acid</json:string><json:string>bovine papillomavirus</json:string><json:string>crystal structure</json:string><json:string>latent infection</json:string><json:string>recognition element</json:string><json:string>ebnal dimer</json:string><json:string>cooperative binding</json:string><json:string>structural homology</json:string><json:string>side chains</json:string><json:string>domain</json:string><json:string>electron density</json:string><json:string>bovine papilloma virus</json:string><json:string>binding sites</json:string><json:string>ebnal dimers</json:string><json:string>nuclear antigen</json:string><json:string>local dyad axis</json:string><json:string>residue</json:string><json:string>binding site</json:string><json:string>structural similarity</json:string><json:string>noncrystallographic axis</json:string><json:string>hydrogen bonds</json:string><json:string>other monomer</json:string><json:string>fusion protein</json:string><json:string>recognition helices</json:string><json:string>cell cycle</json:string><json:string>dimerization domains</json:string><json:string>other proteins</json:string><json:string>ebnal proline loop</json:string><json:string>distinct domains</json:string><json:string>core region</json:string><json:string>ebnal activates</json:string><json:string>dimerization domain</json:string><json:string>inner portion</json:string><json:string>carbon backbones</json:string><json:string>base pairs</json:string><json:string>epsteinbarr virus</json:string><json:string>viral polypeptides</json:string><json:string>viral protein</json:string><json:string>ebnal function</json:string><json:string>reservoir solution</json:string><json:string>space group</json:string><json:string>pcmb data</json:string><json:string>diffraction data</json:string><json:string>ebnai core</json:string><json:string>least squares</json:string><json:string>water molecules</json:string><json:string>refined model</json:string><json:string>sequence conservation</json:string><json:string>sequence requirements</json:string><json:string>replication origin</json:string><json:string>raven press</json:string><json:string>human cells</json:string><json:string>bovine</json:string></teeft></keywords><author><json:item><name>Alexey Bochkarev</name><affiliations><json:string>Institute for Molecular Biology and Biotechnology Cancer Research Group Department of Pathology McMaster University Hamilton, Ontario, Canada L8N 3Z5</json:string></affiliations></json:item><json:item><name>Jean A. Barwell</name><affiliations><json:string>Institute for Molecular Biology and Biotechnology Cancer Research Group Department of Pathology McMaster University Hamilton, Ontario, Canada L8N 3Z5</json:string></affiliations></json:item><json:item><name>Richard A. Pfuetzner</name><affiliations><json:string>Institute for Molecular Biology and Biotechnology Cancer Research Group Department of Pathology McMaster University Hamilton, Ontario, Canada L8N 3Z5</json:string></affiliations></json:item><json:item><name>William Furey, Jr.</name><affiliations><json:string>Veterans Administration Medical Center Biocrystallography Laboratory and Department of Crystallography University of Pittsburgh Pittsburgh, Pennsylvania 15240 USA</json:string></affiliations></json:item><json:item><name>Aled M. Edwards</name><affiliations><json:string>Institute for Molecular Biology and Biotechnology Cancer Research Group Department of Pathology McMaster University Hamilton, Ontario, Canada L8N 3Z5</json:string><json:string>‡ These authors contributed equally to this work.</json:string></affiliations></json:item><json:item><name>Lori Frappier</name><affiliations><json:string>Institute for Molecular Biology and Biotechnology Cancer Research Group Department of Pathology McMaster University Hamilton, Ontario, Canada L8N 3Z5</json:string><json:string>‡ These authors contributed equally to this work.</json:string></affiliations></json:item></author><arkIstex>ark:/67375/6H6-6PVV2SM3-X</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><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.</abstract><qualityIndicators><score>8.608</score><pdfWordCount>6106</pdfWordCount><pdfCharCount>36808</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>8</pdfPageCount><pdfPageSize>612 x 792 pts (letter)</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>134</abstractWordCount><abstractCharCount>867</abstractCharCount><keywordCount>0</keywordCount></qualityIndicators><title>Crystal structure of the DNA-binding domain of the Epstein-Barr virus origin-binding protein EBNA1</title><pmid><json:string>7553871</json:string></pmid><pii><json:string>0092-8674(95)90232-5</json:string></pii><genre><json:string>research-article</json:string></genre><serie><title>Proc. Natl. Acad. Sci. USA</title><language><json:string>unknown</json:string></language><volume>88</volume><pages><first>10875</first><last>10879</last></pages></serie><host><title>Cell</title><language><json:string>unknown</json:string></language><publicationDate>1995</publicationDate><issn><json:string>0092-8674</json:string></issn><pii><json:string>S0092-8674(00)X0437-0</json:string></pii><volume>83</volume><issue>1</issue><pages><first>39</first><last>46</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>8834</json:string><json:string>1995</json:string></date><geogName></geogName><orgName><json:string>National Cancer Institute of Canada</json:string><json:string>Medical Research Council of Canada</json:string><json:string>Howard Hughes Medical Institute and Department of Molecular Biophysics and Biochemistry</json:string><json:string>NCI</json:string><json:string>Research Scholar of the MRC</json:string><json:string>Administration Medical Center Biocrystallography Laboratory and Department of Crystallography University of Pittsburgh Pittsburgh, Pennsylvania</json:string><json:string>Research Scientist of the NCI</json:string><json:string>MRC</json:string><json:string>Yale University</json:string></orgName><orgName_funder></orgName_funder><orgName_provider></orgName_provider><persName><json:string>Lori Frappier</json:string><json:string>J. Rim</json:string><json:string>R. Read</json:string><json:string>A. Zdanov</json:string><json:string>A. T. Briinger</json:string><json:string>D. Yang</json:string><json:string>William Furey</json:string><json:string>Z. Otwinowski</json:string><json:string>C. Arrowsmith</json:string><json:string>Aled M. Edwards</json:string><json:string>J. Rini</json:string><json:string>S. Darst</json:string><json:string>Richard A. Pfuetzner</json:string><json:string>D. Chasman</json:string><json:string>F. Sicheri</json:string><json:string>J. Pflugrath</json:string><json:string>Jean A. Barwell</json:string><json:string>Hayward</json:string></persName><placeName><json:string>Madison</json:string><json:string>CT</json:string><json:string>WI</json:string><json:string>New Haven</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Mohr et al., 1990</json:string><json:string>Hendrickson and Konnert, 19801</json:string><json:string>Chen et al., 1994</json:string><json:string>Miller, 1990</json:string><json:string>Frappier and O ’ Donnell, 1991</json:string><json:string>Yang et al., 1991</json:string><json:string>Studier et al., 1990</json:string><json:string>Yates et al., 1985</json:string><json:string>Ustav et al., 1991</json:string><json:string>Chen et al., 1993</json:string><json:string>Harrison et al., 1994</json:string><json:string>Muchardt and Yaniv, 1993</json:string><json:string>Adams, 1987</json:string><json:string>Reisman et al., 1985</json:string><json:string>Lupton and Levine, 1985</json:string><json:string>Giri and Yaniv, 1988</json:string><json:string>Hearing et al., 1992</json:string><json:string>Rawlins et al., 1985</json:string><json:string>Reisman and Sugden, 1986</json:string><json:string>Barwell et al., 1995</json:string><json:string>Krysan et al., 1989</json:string><json:string>Ustav and Stenlund, 1991</json:string><json:string>Hsieh et al., 1993</json:string><json:string>Friedman et al., 1995</json:string><json:string>Goldsmith et al., 1993</json:string><json:string>Furey and Swaminathan, 1995</json:string><json:string>Steger et al., 1995</json:string><json:string>Furey et al., 1982</json:string><json:string>Frappier et al., 1994</json:string><json:string>Yates and Guan, 1991</json:string><json:string>Ambinder et al., 1991</json:string><json:string>Roizmann and Sears, 1990</json:string><json:string>Sugden and Warren, 1989</json:string><json:string>reviewed by Klein, 1989</json:string><json:string>Yang et al., 1993</json:string><json:string>Summers et al.</json:string><json:string>Seo et al., 1993</json:string><json:string>Hegde et al., 1992</json:string><json:string>Jones et al., 1991</json:string><json:string>Prakash et al., 1992</json:string><json:string>Ambinder et al., 1990</json:string><json:string>Frappier and O ’ Donnell, 1992</json:string><json:string>Bonne-Andrea et al., 1995</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-6PVV2SM3-X</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - cell biology</json:string><json:string>2 - biochemistry & molecular biology</json:string></wos><scienceMetrix><json:string>1 - health sciences</json:string><json:string>2 - biomedical research</json:string><json:string>3 - developmental biology</json:string></scienceMetrix><scopus><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - General Biochemistry, Genetics and Molecular 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type="first">Alexey</forename><surname>Bochkarev</surname></persName><affiliation>Institute for Molecular Biology and Biotechnology Cancer Research Group Department of Pathology McMaster University Hamilton, Ontario, Canada L8N 3Z5</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Jean A.</forename><surname>Barwell</surname></persName><affiliation>Institute for Molecular Biology and Biotechnology Cancer Research Group Department of Pathology McMaster University Hamilton, Ontario, Canada L8N 3Z5</affiliation></author><author xml:id="author-0002"><persName><forename type="first">Richard A.</forename><surname>Pfuetzner</surname></persName><affiliation>Institute for Molecular Biology and Biotechnology Cancer Research Group Department of Pathology McMaster University Hamilton, Ontario, Canada L8N 3Z5</affiliation></author><author xml:id="author-0003"><persName><forename type="first">William</forename><surname>Furey, Jr.</surname></persName><affiliation>Veterans Administration Medical Center Biocrystallography Laboratory and Department of Crystallography University of Pittsburgh Pittsburgh, Pennsylvania 15240 USA</affiliation></author><author xml:id="author-0004"><persName><forename type="first">Aled M.</forename><surname>Edwards</surname></persName><affiliation>Institute for Molecular Biology and Biotechnology Cancer Research Group Department of Pathology McMaster University Hamilton, Ontario, Canada L8N 3Z5</affiliation><affiliation>‡ These authors contributed equally to this work.</affiliation></author><author xml:id="author-0005"><persName><forename type="first">Lori</forename><surname>Frappier</surname></persName><affiliation>Institute for Molecular Biology and Biotechnology Cancer Research Group Department of Pathology McMaster University Hamilton, Ontario, Canada L8N 3Z5</affiliation><affiliation>‡ These authors contributed equally to this work.</affiliation></author><idno type="istex">4CF9DDD9CD8B61733A7B04D6B8B0523FDDAB2E09</idno><idno type="ark">ark:/67375/6H6-6PVV2SM3-X</idno><idno type="DOI">10.1016/0092-8674(95)90232-5</idno><idno type="PII">0092-8674(95)90232-5</idno></analytic><monogr><title level="j">Cell</title><title level="j" type="abbrev">CELL</title><idno type="pISSN">0092-8674</idno><idno type="PII">S0092-8674(00)X0437-0</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="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></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1995</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>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.</p></abstract></profileDesc><revisionDesc><change when="1995-08-17">Modified</change><change when="1995">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-6PVV2SM3-X/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla"><item-info><jid>CELL</jid><aid>95902325</aid><ce:pii>0092-8674(95)90232-5</ce:pii><ce:doi>10.1016/0092-8674(95)90232-5</ce:doi><ce:copyright type="unknown" year="1995"></ce:copyright></item-info><head><ce:dochead><ce:textfn>Article</ce:textfn></ce:dochead><ce:title>Crystal structure of the DNA-binding domain of the Epstein-Barr virus origin-binding protein EBNA1</ce:title><ce:author-group><ce:author><ce:given-name>Alexey</ce:given-name><ce:surname>Bochkarev</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Jean A.</ce:given-name><ce:surname>Barwell</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Richard A.</ce:given-name><ce:surname>Pfuetzner</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>William</ce:given-name><ce:surname>Furey</ce:surname><ce:suffix>Jr.</ce:suffix><ce:cross-ref refid="AFF2"><ce:sup>†</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Aled M.</ce:given-name><ce:surname>Edwards</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref><ce:cross-ref refid="FN1"><ce:sup>‡</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Lori</ce:given-name><ce:surname>Frappier</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref><ce:cross-ref refid="FN1"><ce:sup>‡</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>∗</ce:label><ce:textfn>Institute for Molecular Biology and Biotechnology Cancer Research Group Department of Pathology McMaster University Hamilton, Ontario, Canada L8N 3Z5</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>†</ce:label><ce:textfn>Veterans Administration Medical Center Biocrystallography Laboratory and Department of Crystallography University of Pittsburgh Pittsburgh, Pennsylvania 15240 USA</ce:textfn></ce:affiliation><ce:footnote id="FN1"><ce:label>‡</ce:label><ce:note-para>These authors contributed equally to this work.</ce:note-para></ce:footnote></ce:author-group><ce:date-received day="13" month="7" year="1995"></ce:date-received><ce:date-revised day="17" month="8" year="1995"></ce:date-revised><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>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.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Crystal structure of the DNA-binding domain of the Epstein-Barr virus origin-binding protein EBNA1</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Crystal structure of the DNA-binding domain of the Epstein-Barr virus origin-binding protein EBNA1</title></titleInfo><name type="personal"><namePart type="given">Alexey</namePart><namePart type="family">Bochkarev</namePart><affiliation>Institute for Molecular Biology and Biotechnology Cancer Research Group Department of Pathology McMaster University Hamilton, Ontario, Canada L8N 3Z5</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Jean A.</namePart><namePart type="family">Barwell</namePart><affiliation>Institute for Molecular Biology and Biotechnology Cancer Research Group Department of Pathology McMaster University Hamilton, Ontario, Canada L8N 3Z5</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Richard A.</namePart><namePart type="family">Pfuetzner</namePart><affiliation>Institute for Molecular Biology and Biotechnology Cancer Research Group Department of Pathology McMaster University Hamilton, Ontario, Canada L8N 3Z5</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">William</namePart><namePart type="family">Furey, Jr.</namePart><affiliation>Veterans Administration Medical Center Biocrystallography Laboratory and Department of Crystallography University of Pittsburgh Pittsburgh, Pennsylvania 15240 USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Aled M.</namePart><namePart type="family">Edwards</namePart><affiliation>Institute for Molecular Biology and Biotechnology Cancer Research Group Department of Pathology McMaster University Hamilton, Ontario, Canada L8N 3Z5</affiliation><affiliation>‡ These authors contributed equally to this work.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Lori</namePart><namePart type="family">Frappier</namePart><affiliation>Institute for Molecular Biology and Biotechnology Cancer Research Group Department of Pathology McMaster University Hamilton, Ontario, Canada L8N 3Z5</affiliation><affiliation>‡ These authors contributed equally to this work.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1995</dateIssued><dateModified encoding="w3cdtf">1995-08-17</dateModified><copyrightDate encoding="w3cdtf">1995</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract 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.</abstract><note type="content">Section title: Article</note><relatedItem type="host"><titleInfo><title>Cell</title></titleInfo><titleInfo type="abbreviated"><title>CELL</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1995</dateIssued></originInfo><identifier type="ISSN">0092-8674</identifier><identifier type="PII">S0092-8674(00)X0437-0</identifier><part><date>1995</date><detail type="volume"><number>83</number><caption>vol.</caption></detail><detail type="issue"><number>1</number><caption>no.</caption></detail><extent unit="issue-pages"><start>1</start><end>155</end></extent><extent unit="pages"><start>39</start><end>46</end></extent></part></relatedItem><identifier type="istex">4CF9DDD9CD8B61733A7B04D6B8B0523FDDAB2E09</identifier><identifier type="ark">ark:/67375/6H6-6PVV2SM3-X</identifier><identifier type="DOI">10.1016/0092-8674(95)90232-5</identifier><identifier type="PII">0092-8674(95)90232-5</identifier><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-6PVV2SM3-X/record.json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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