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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Crystal structure of the post‐fusion core of the <italic>Human coronavirus 229E</italic> spike protein at 1.86 Å resolution</title><author><name sortKey="Yan, Lei" sort="Yan, Lei" uniqKey="Yan L" first="Lei" last="Yan">Lei Yan</name><affiliation><nlm:aff id="AYD2UD5004-aff-a1"></nlm:aff></affiliation><affiliation><nlm:aff id="AYD2UD5004-aff-a2"></nlm:aff></affiliation><affiliation><nlm:aff id="AYD2UD5004-aff-a3"></nlm:aff></affiliation><affiliation><nlm:aff id="AYD2UD5004-aff-a4"></nlm:aff></affiliation></author><author><name sortKey="Meng, Bing" sort="Meng, Bing" uniqKey="Meng B" first="Bing" last="Meng">Bing Meng</name><affiliation><nlm:aff id="AYD2UD5004-aff-a1"></nlm:aff></affiliation></author><author><name sortKey="Xiang, Jiangchao" sort="Xiang, Jiangchao" uniqKey="Xiang J" first="Jiangchao" last="Xiang">Jiangchao Xiang</name><affiliation><nlm:aff id="AYD2UD5004-aff-a1"></nlm:aff></affiliation><affiliation><nlm:aff id="AYD2UD5004-aff-a2"></nlm:aff></affiliation><affiliation><nlm:aff id="AYD2UD5004-aff-a3"></nlm:aff></affiliation><affiliation><nlm:aff id="AYD2UD5004-aff-a4"></nlm:aff></affiliation></author><author><name sortKey="Wilson, Ian A" sort="Wilson, Ian A" uniqKey="Wilson I" first="Ian A." last="Wilson">Ian A. Wilson</name><affiliation><nlm:aff id="AYD2UD5004-aff-a1"></nlm:aff></affiliation><affiliation><nlm:aff id="AYD2UD5004-aff-a5"></nlm:aff></affiliation></author><author><name sortKey="Yang, Bei" sort="Yang, Bei" uniqKey="Yang B" first="Bei" last="Yang">Bei Yang</name><affiliation><nlm:aff id="AYD2UD5004-aff-a1"></nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">30198895</idno><idno type="pmc">6130466</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6130466</idno><idno type="RBID">PMC:6130466</idno><idno type="doi">10.1107/S2059798318008318</idno><date when="2018">2018</date><idno type="wicri:Area/Pmc/Corpus">000978</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000978</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Crystal structure of the post‐fusion core of the <italic>Human coronavirus 229E</italic> spike protein at 1.86 Å resolution</title><author><name sortKey="Yan, Lei" sort="Yan, Lei" uniqKey="Yan L" first="Lei" last="Yan">Lei Yan</name><affiliation><nlm:aff id="AYD2UD5004-aff-a1"></nlm:aff></affiliation><affiliation><nlm:aff id="AYD2UD5004-aff-a2"></nlm:aff></affiliation><affiliation><nlm:aff id="AYD2UD5004-aff-a3"></nlm:aff></affiliation><affiliation><nlm:aff id="AYD2UD5004-aff-a4"></nlm:aff></affiliation></author><author><name sortKey="Meng, Bing" sort="Meng, Bing" uniqKey="Meng B" first="Bing" last="Meng">Bing Meng</name><affiliation><nlm:aff id="AYD2UD5004-aff-a1"></nlm:aff></affiliation></author><author><name sortKey="Xiang, Jiangchao" sort="Xiang, Jiangchao" uniqKey="Xiang J" first="Jiangchao" last="Xiang">Jiangchao Xiang</name><affiliation><nlm:aff id="AYD2UD5004-aff-a1"></nlm:aff></affiliation><affiliation><nlm:aff id="AYD2UD5004-aff-a2"></nlm:aff></affiliation><affiliation><nlm:aff id="AYD2UD5004-aff-a3"></nlm:aff></affiliation><affiliation><nlm:aff id="AYD2UD5004-aff-a4"></nlm:aff></affiliation></author><author><name sortKey="Wilson, Ian A" sort="Wilson, Ian A" uniqKey="Wilson I" first="Ian A." last="Wilson">Ian A. Wilson</name><affiliation><nlm:aff id="AYD2UD5004-aff-a1"></nlm:aff></affiliation><affiliation><nlm:aff id="AYD2UD5004-aff-a5"></nlm:aff></affiliation></author><author><name sortKey="Yang, Bei" sort="Yang, Bei" uniqKey="Yang B" first="Bei" last="Yang">Bei Yang</name><affiliation><nlm:aff id="AYD2UD5004-aff-a1"></nlm:aff></affiliation></author></analytic><series><title level="j">Acta Crystallographica. Section D, Structural Biology</title><idno type="eISSN">2059-7983</idno><imprint><date when="2018">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><italic>Human coronavirus 229E</italic> (HCoV‐229E) usually causes mild upper respiratory infections in heathy adults, but may lead to severe complications or mortality in individuals with weakened immune systems. Virus entry of HCoV‐229E is mediated by its spike (S) protein, where the S1 domain facilitates attachment to host cells and the S2 domain is involved in subsequent fusion of the virus and host membranes. During the fusion process, two heptad repeats, HR1 and HR2, in the S2 domain assemble into a six‐helix membrane‐fusion structure termed the fusion core. Here, the complete fusion‐core structure of HCoV‐229E has been determined at 1.86 Å resolution, representing the most complete post‐fusion conformation thus far among published human alphacoronavirus (α‐HCoV) fusion‐core structures. The overall structure of the HCoV‐229E fusion core is similar to those of SARS, MERS and HCoV‐NL63, but the packing of its 3HR1 core differs from those of SARS and MERS in that it contains more noncanonical `x' and `da' layers. Side‐by‐side electrostatic surface comparisons reveal that the electrostatic surface potentials are opposite in α‐HCoVs and β‐HCoVs at certain positions and that the HCoV‐229E surface also appears to be the most hydrophobic among the various HCoVs. In addition to the highly conserved hydrophobic interactions between HR1 and HR2, some polar and electrostatic interactions are also well preserved across different HCoVs. This study adds to the structural profiling of HCoVs to aid in the structure‐based design of pan‐coronavirus small molecules or peptides to inhibit viral fusion.</p></div></front></TEI><pmc article-type="research-article"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Acta Crystallogr D Struct Biol</journal-id><journal-id journal-id-type="iso-abbrev">Acta Crystallogr D Struct Biol</journal-id><journal-id journal-id-type="doi">10.1107/S20597983</journal-id><journal-id journal-id-type="publisher-id">AYD2</journal-id><journal-title-group><journal-title>Acta Crystallographica. Section D, Structural Biology</journal-title></journal-title-group><issn pub-type="epub">2059-7983</issn><publisher><publisher-name>International Union of Crystallography</publisher-name><publisher-loc>5 Abbey Square, Chester, Cheshire CH1 2HU, England</publisher-loc></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">30198895</article-id><article-id pub-id-type="pmc">6130466</article-id><article-id pub-id-type="doi">10.1107/S2059798318008318</article-id><article-id pub-id-type="publisher-id">AYD2UD5004</article-id><article-id pub-id-type="other">UD5004</article-id><article-categories><subj-group subj-group-type="overline"><subject>Research Papers</subject></subj-group><subj-group subj-group-type="heading"><subject>Research Papers</subject></subj-group></article-categories><title-group><article-title>Crystal structure of the post‐fusion core of the <italic>Human coronavirus 229E</italic> spike protein at 1.86 Å resolution</article-title><alt-title alt-title-type="right-running-head">Post‐fusion core of the Human coronavirus 229E spike protein</alt-title></title-group><contrib-group><contrib id="AYD2UD5004-cr-1" contrib-type="author"><name><surname>Yan</surname><given-names>Lei</given-names></name><xref ref-type="aff" rid="AYD2UD5004-aff-a1"><sup>1</sup></xref><xref ref-type="aff" rid="AYD2UD5004-aff-a2"><sup>2</sup></xref><xref ref-type="aff" rid="AYD2UD5004-aff-a3"><sup>3</sup></xref><xref ref-type="aff" rid="AYD2UD5004-aff-a4"><sup>4</sup></xref></contrib><contrib id="AYD2UD5004-cr-2" contrib-type="author"><name><surname>Meng</surname><given-names>Bing</given-names></name><xref ref-type="aff" rid="AYD2UD5004-aff-a1"><sup>1</sup></xref></contrib><contrib id="AYD2UD5004-cr-3" contrib-type="author"><name><surname>Xiang</surname><given-names>Jiangchao</given-names></name><xref ref-type="aff" rid="AYD2UD5004-aff-a1"><sup>1</sup></xref><xref ref-type="aff" rid="AYD2UD5004-aff-a2"><sup>2</sup></xref><xref ref-type="aff" rid="AYD2UD5004-aff-a3"><sup>3</sup></xref><xref ref-type="aff" rid="AYD2UD5004-aff-a4"><sup>4</sup></xref></contrib><contrib id="AYD2UD5004-cr-4" contrib-type="author" corresp="yes"><name><surname>Wilson</surname><given-names>Ian A.</given-names></name><xref ref-type="aff" rid="AYD2UD5004-aff-a1"><sup>1</sup></xref><xref ref-type="aff" rid="AYD2UD5004-aff-a5"><sup>5</sup></xref><address><email>wilson@scripps.edu</email></address></contrib><contrib id="AYD2UD5004-cr-5" contrib-type="author" corresp="yes"><name><surname>Yang</surname><given-names>Bei</given-names></name><xref ref-type="aff" rid="AYD2UD5004-aff-a1"><sup>1</sup></xref><address><email>yangbei@shanghaitech.edu.cn</email></address></contrib></contrib-group><aff id="AYD2UD5004-aff-a1"><label><sup>1</sup></label>Shanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, 393 Middle Huaxia Road, Shanghai201210, People's Republic of China</aff><aff id="AYD2UD5004-aff-a2"><label><sup>2</sup></label>School of Life Science and Technology, ShanghaiTech University, 393 Middle Huaxia Road, Shanghai201210, People's Republic of China</aff><aff id="AYD2UD5004-aff-a3"><label><sup>3</sup></label>Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, 320 Yueyang Road, Shanghai200031, People's Republic of China</aff><aff id="AYD2UD5004-aff-a4"><label><sup>4</sup></label>University of Chinese Academy of Sciences, 19A Yuquan Road, Beijing100049, People's Republic of China</aff><aff id="AYD2UD5004-aff-a5"><label><sup>5</sup></label>Department of Integrative Structural and Computational Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, BCC206, La Jolla, CA92037, USA</aff><author-notes><corresp id="correspondenceTo"><label>*</label>Ian A. Wilson, e-mail: <email>wilson@scripps.edu</email>; Bei Yang, e-mail: <email>yangbei@shanghaitech.edu.cn</email></corresp></author-notes><pub-date pub-type="epub"><day>10</day><month>9</month><year>2018</year></pub-date><pub-date pub-type="ppub"><month>9</month><year>2018</year></pub-date><volume>74</volume><issue>9</issue><issue-id pub-id-type="doi">10.1107/S20597983740900</issue-id><fpage>841</fpage><lpage>851</lpage><history><date date-type="received"><day>07</day><month>4</month><year>2018</year></date><date date-type="accepted"><day>05</day><month>6</month><year>2018</year></date></history><permissions><copyright-statement content-type="article-copyright">© Yan et al. 2018</copyright-statement><license license-type="creativeCommonsBy"><license-p>This is an open‐access article distributed under the terms of the <ext-link ext-link-type="uri" xlink:href="http://creativecommons.org/licenses/by/2.0/uk/legalcode">http://creativecommons.org/licenses/by/2.0/uk/legalcode</ext-link>, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.</license-p></license></permissions><self-uri content-type="pdf" xlink:href="file:AYD2-74-841.pdf"></self-uri><abstract><p><italic>Human coronavirus 229E</italic> (HCoV‐229E) usually causes mild upper respiratory infections in heathy adults, but may lead to severe complications or mortality in individuals with weakened immune systems. Virus entry of HCoV‐229E is mediated by its spike (S) protein, where the S1 domain facilitates attachment to host cells and the S2 domain is involved in subsequent fusion of the virus and host membranes. During the fusion process, two heptad repeats, HR1 and HR2, in the S2 domain assemble into a six‐helix membrane‐fusion structure termed the fusion core. Here, the complete fusion‐core structure of HCoV‐229E has been determined at 1.86 Å resolution, representing the most complete post‐fusion conformation thus far among published human alphacoronavirus (α‐HCoV) fusion‐core structures. The overall structure of the HCoV‐229E fusion core is similar to those of SARS, MERS and HCoV‐NL63, but the packing of its 3HR1 core differs from those of SARS and MERS in that it contains more noncanonical `x' and `da' layers. Side‐by‐side electrostatic surface comparisons reveal that the electrostatic surface potentials are opposite in α‐HCoVs and β‐HCoVs at certain positions and that the HCoV‐229E surface also appears to be the most hydrophobic among the various HCoVs. In addition to the highly conserved hydrophobic interactions between HR1 and HR2, some polar and electrostatic interactions are also well preserved across different HCoVs. This study adds to the structural profiling of HCoVs to aid in the structure‐based design of pan‐coronavirus small molecules or peptides to inhibit viral fusion.</p></abstract><abstract abstract-type="graphical"><p>The complete post‐fusion core structure of the <italic>Human coronavirus 229E</italic> spike protein was determined at 1.86 Å resolution. Comparison of the interactions between heptad repeats HR1 and HR2 in different human coronaviruses reveals some differences, which should be taken into consideration when designing pan‐coronavirus HR2‐mimicking inhibitors that target HR1.<boxed-text position="anchor" content-type="graphic" orientation="portrait"><graphic xlink:href="AYD2-74-841-g001.jpg" position="anchor" id="nlm-graphic-1" orientation="portrait"></graphic></boxed-text></p></abstract><kwd-group><kwd id="AYD2UD5004-kwd-1">coronavirus</kwd><kwd id="AYD2UD5004-kwd-2">HCoV‐229E</kwd><kwd id="AYD2UD5004-kwd-3">spike protein</kwd><kwd id="AYD2UD5004-kwd-4">post‐fusion core</kwd><kwd id="AYD2UD5004-kwd-5">X‐ray structure</kwd><kwd id="AYD2UD5004-kwd-6">SARS</kwd><kwd id="AYD2UD5004-kwd-7">MERS</kwd></kwd-group><counts><fig-count count="0"></fig-count><table-count count="0"></table-count><page-count count="10"></page-count><word-count count="0"></word-count></counts><custom-meta-group><custom-meta><meta-name>source-schema-version-number</meta-name><meta-value>2.0</meta-value></custom-meta><custom-meta><meta-name>cover-date</meta-name><meta-value>September 2018</meta-value></custom-meta><custom-meta><meta-name>details-of-publishers-convertor</meta-name><meta-value>Converter:WILEY_ML3GV2_TO_JATSPMC version:5.8.0 mode:remove_FC converted:15.04.2020</meta-value></custom-meta></custom-meta-group></article-meta></front><body><p>The full text for this article, hosted at <ext-link ext-link-type="uri" xlink:href="http://journals.iucr.org">http://journals.iucr.org</ext-link>, is unavailable due to technical difficulties.</p><sec sec-type="supplementary-material"><title>Supporting information</title><supplementary-material content-type="local-data"><p>Supporting information for this article can be found <ext-link ext-link-type="uri" xlink:href="http://scripts.iucr.org/cgi-bin/paper?ud5004">http://scripts.iucr.org/cgi-bin/paper?ud5004</ext-link></p></supplementary-material></sec></body></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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