Crystallization and Structural Determination of the Receptor-Binding Domain of MERS-CoV Spike Glycoprotein
Identifieur interne : 000178 ( Pmc/Curation ); précédent : 000177; suivant : 000179Crystallization and Structural Determination of the Receptor-Binding Domain of MERS-CoV Spike Glycoprotein
Auteurs :Source :
- MERS Coronavirus ; 2019.
Abstract
Three-dimensional structures of the receptor-binding domain (RBD) of MERS-CoV spike glycoprotein bound to cellular receptor and monoclonal antibodies (mAbs) have been determined by X-ray crystallography, providing structural information about receptor recognition and neutralizing mechanisms of mAbs at the atomic level. In this chapter, we describe the purification, crystallization, and structure determination of the MERS-CoV RBD.
Url:
DOI: 10.1007/978-1-0716-0211-9_4
PubMed: 31883086
PubMed Central: 7123399
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<front><div type="abstract" xml:lang="en"><p id="Par1">Three-dimensional structures of the receptor-binding domain (RBD) of MERS-CoV spike glycoprotein bound to cellular receptor and monoclonal antibodies (mAbs) have been determined by X-ray crystallography, providing structural information about receptor recognition and neutralizing mechanisms of mAbs at the atomic level. In this chapter, we describe the purification, crystallization, and structure determination of the MERS-CoV RBD.</p>
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<isbn publication-format="print">978-1-0716-0210-2</isbn>
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<title-group><article-title>Crystallization and Structural Determination of the Receptor-Binding Domain of MERS-CoV Spike Glycoprotein</article-title>
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<contrib-group content-type="book editors"><contrib contrib-type="editor"><name><surname>Vijay</surname>
<given-names>Rahul</given-names>
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<address><email>rahul-vijay@uiowa.edu</email>
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<institution>Department of Microbiology and Immunology,</institution>
<institution>University of Iowa,</institution>
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Iowa City, IA USA</aff>
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<contrib-group><contrib contrib-type="author"><name><surname>Zhou</surname>
<given-names>Haixia</given-names>
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<contrib contrib-type="author"><name><surname>Zhang</surname>
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<contrib contrib-type="author" corresp="yes"><name><surname>Wang</surname>
<given-names>Xinquan</given-names>
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<address><email>xinquanwang@mail.tsinghua.edu.cn</email>
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<institution>School of Life Sciences,</institution>
<institution>Tsinghua University,</institution>
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Beijing, China</aff>
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<pub-date pub-type="epub"><day>14</day>
<month>9</month>
<year>2019</year>
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<pub-date pub-type="collection"><year>2020</year>
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<volume>2099</volume>
<fpage>39</fpage>
<lpage>50</lpage>
<permissions><copyright-statement>© Springer Science+Business Media, LLC, part of Springer Nature 2020</copyright-statement>
<license><license-p>This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic.</license-p>
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<abstract id="Abs1"><p id="Par1">Three-dimensional structures of the receptor-binding domain (RBD) of MERS-CoV spike glycoprotein bound to cellular receptor and monoclonal antibodies (mAbs) have been determined by X-ray crystallography, providing structural information about receptor recognition and neutralizing mechanisms of mAbs at the atomic level. In this chapter, we describe the purification, crystallization, and structure determination of the MERS-CoV RBD.</p>
</abstract>
<kwd-group xml:lang="en"><title>Key words</title>
<kwd>X-ray crystallography</kwd>
<kwd>MERS-CoV</kwd>
<kwd>Spike</kwd>
<kwd>RBD</kwd>
<kwd>Crystallization</kwd>
<kwd>Structure determination</kwd>
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<meta-value>© Springer Science+Business Media, LLC, part of Springer Nature 2020</meta-value>
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