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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Activation and maturation of SARS-CoV main protease</title>
<author><name sortKey="Xia, Bin" sort="Xia, Bin" uniqKey="Xia B" first="Bin" last="Xia">Bin Xia</name>
<affiliation><nlm:aff id="Aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Kang, Xue" sort="Kang, Xue" uniqKey="Kang X" first="Xue" last="Kang">Xue Kang</name>
<affiliation><nlm:aff id="Aff1"></nlm:aff>
</affiliation>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PMC</idno>
<idno type="pmid">21533772</idno>
<idno type="pmc">4875205</idno>
<idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4875205</idno>
<idno type="RBID">PMC:4875205</idno>
<idno type="doi">10.1007/s13238-011-1034-1</idno>
<date when="2011">2011</date>
<idno type="wicri:Area/Pmc/Corpus">000169</idno>
<idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000169</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Activation and maturation of SARS-CoV main protease</title>
<author><name sortKey="Xia, Bin" sort="Xia, Bin" uniqKey="Xia B" first="Bin" last="Xia">Bin Xia</name>
<affiliation><nlm:aff id="Aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Kang, Xue" sort="Kang, Xue" uniqKey="Kang X" first="Xue" last="Kang">Xue Kang</name>
<affiliation><nlm:aff id="Aff1"></nlm:aff>
</affiliation>
</author>
</analytic>
<series><title level="j">Protein & Cell</title>
<idno type="ISSN">1674-800X</idno>
<idno type="eISSN">1674-8018</idno>
<imprint><date when="2011">2011</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass></textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en"><p>The worldwide outbreak of the severe acute respiratory syndrome (SARS) in 2003 was due to the transmission of SARS coronavirus (SARS-CoV). The main protease (M<sup>pro</sup>
) of SARS-CoV is essential for the viral life cycle, and is considered to be an attractive target of anti-SARS drug development. As a key enzyme for proteolytic processing of viral polyproteins to produce functional non-structure proteins, M<sup>pro</sup>
is first auto-cleaved out of polyproteins. The monomeric form of M<sup>pro</sup>
is enzymatically inactive, and it is activated through homo-dimerization which is strongly affected by extra residues to both ends of the mature enzyme. This review provides a summary of the related literatures on the study of the quaternary structure, activation, and self-maturation of M<sup>pro</sup>
over the past years.</p>
</div>
</front>
</TEI>
<pmc article-type="review-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Protein Cell</journal-id>
<journal-id journal-id-type="iso-abbrev">Protein Cell</journal-id>
<journal-title-group><journal-title>Protein & Cell</journal-title>
</journal-title-group>
<issn pub-type="ppub">1674-800X</issn>
<issn pub-type="epub">1674-8018</issn>
<publisher><publisher-name>Higher Education Press</publisher-name>
<publisher-loc>Beijing</publisher-loc>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">21533772</article-id>
<article-id pub-id-type="pmc">4875205</article-id>
<article-id pub-id-type="publisher-id">1034</article-id>
<article-id pub-id-type="doi">10.1007/s13238-011-1034-1</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Review</subject>
</subj-group>
</article-categories>
<title-group><article-title>Activation and maturation of SARS-CoV main protease</article-title>
</title-group>
<contrib-group><contrib contrib-type="author" corresp="yes"><name><surname>Xia</surname>
<given-names>Bin</given-names>
</name>
<address><email>binxia@pku.edu.cn</email>
</address>
<xref ref-type="aff" rid="Aff1"></xref>
</contrib>
<contrib contrib-type="author"><name><surname>Kang</surname>
<given-names>Xue</given-names>
</name>
<xref ref-type="aff" rid="Aff1"></xref>
</contrib>
<aff id="Aff1"><institution-wrap><institution-id institution-id-type="GRID">grid.11135.37</institution-id>
<institution-id institution-id-type="ISNI">0000000122569319</institution-id>
<institution>Beijing Nuclear Magnetic Resonance Center, College of Chemistry and Molecular Engineering, and School of Life Sciences,</institution>
<institution>Peking University,</institution>
</institution-wrap>
Beijing, 100871 China</aff>
</contrib-group>
<pub-date pub-type="epub"><day>28</day>
<month>4</month>
<year>2011</year>
</pub-date>
<pub-date pub-type="ppub"><month>4</month>
<year>2011</year>
</pub-date>
<volume>2</volume>
<issue>4</issue>
<fpage>282</fpage>
<lpage>290</lpage>
<history><date date-type="received"><day>21</day>
<month>3</month>
<year>2011</year>
</date>
<date date-type="accepted"><day>7</day>
<month>4</month>
<year>2011</year>
</date>
</history>
<permissions><copyright-statement>© Higher Education Press and Springer-Verlag Berlin Heidelberg 2011</copyright-statement>
</permissions>
<abstract id="Abs1"><p>The worldwide outbreak of the severe acute respiratory syndrome (SARS) in 2003 was due to the transmission of SARS coronavirus (SARS-CoV). The main protease (M<sup>pro</sup>
) of SARS-CoV is essential for the viral life cycle, and is considered to be an attractive target of anti-SARS drug development. As a key enzyme for proteolytic processing of viral polyproteins to produce functional non-structure proteins, M<sup>pro</sup>
is first auto-cleaved out of polyproteins. The monomeric form of M<sup>pro</sup>
is enzymatically inactive, and it is activated through homo-dimerization which is strongly affected by extra residues to both ends of the mature enzyme. This review provides a summary of the related literatures on the study of the quaternary structure, activation, and self-maturation of M<sup>pro</sup>
over the past years.</p>
</abstract>
<kwd-group xml:lang="en"><title>Keywords</title>
<kwd>severe acute respiratory syndrome</kwd>
<kwd>M<sup>pro</sup>
</kwd>
<kwd>structure</kwd>
<kwd>dimerization</kwd>
</kwd-group>
<custom-meta-group><custom-meta><meta-name>issue-copyright-statement</meta-name>
<meta-value>© HEP and Springer 2011</meta-value>
</custom-meta>
</custom-meta-group>
</article-meta>
</front>
</pmc>
</record>
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