Crystallization and Structural Determination of the Receptor-Binding Domain of MERS-CoV Spike Glycoprotein.
Identifieur interne : 000314 ( PubMed/Corpus ); précédent : 000313; suivant : 000315Crystallization and Structural Determination of the Receptor-Binding Domain of MERS-CoV Spike Glycoprotein.
Auteurs : Haixia Zhou ; Shuyuan Zhang ; Xinquan WangSource :
- Methods in molecular biology (Clifton, N.J.) [ 1940-6029 ] ; 2020.
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.
DOI: 10.1007/978-1-0716-0211-9_4
PubMed: 31883086
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<front><div type="abstract" xml:lang="en">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.</div>
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<ReferenceList><Reference><Citation>J Virol. 2018 Apr 27;92(10):</Citation>
<ArticleIdList><ArticleId IdType="pubmed">29514901</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Nat Commun. 2015 Sep 15;6:8223</Citation>
<ArticleIdList><ArticleId IdType="pubmed">26370782</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Nature. 2013 Aug 8;500(7461):227-31</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23831647</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Nat Commun. 2015 Jul 28;6:7712</Citation>
<ArticleIdList><ArticleId IdType="pubmed">26218507</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Methods Enzymol. 1997;276:307-26</Citation>
<ArticleIdList><ArticleId IdType="pubmed">27754618</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Cell Rep. 2018 Jul 10;24(2):441-452</Citation>
<ArticleIdList><ArticleId IdType="pubmed">29996104</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Infect Dis. 2018 Sep 8;218(8):1249-1260</Citation>
<ArticleIdList><ArticleId IdType="pubmed">29846635</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2126-32</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15572765</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Cell Res. 2013 Aug;23(8):986-93</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23835475</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2002 Nov;58(Pt 11):1948-54</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12393927</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Sci Rep. 2015 Aug 18;5:13133</Citation>
<ArticleIdList><ArticleId IdType="pubmed">26281793</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Nat Commun. 2016 Nov 22;7:13473</Citation>
<ArticleIdList><ArticleId IdType="pubmed">27874853</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Appl Crystallogr. 2007 Aug 1;40(Pt 4):658-674</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19461840</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
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