SARS-CoV heptad repeat 2 is a trimer of parallel helices.
Identifieur interne : 001472 ( PubMed/Curation ); précédent : 001471; suivant : 001473SARS-CoV heptad repeat 2 is a trimer of parallel helices.
Auteurs : Jessica Celigoy [États-Unis] ; Benjamin Ramirez ; Michael CaffreySource :
- Protein science : a publication of the Protein Society [ 1469-896X ] ; 2011.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Viral Envelope Proteins.
- chemical : Spin Labels.
- chemistry : SARS Virus.
- virology : Severe Acute Respiratory Syndrome.
- Models, Molecular, Nuclear Magnetic Resonance, Biomolecular, Protein Multimerization, Protein Structure, Secondary.
Abstract
In severe acute respiratory syndrome coronavirus, the envelope heptad repeat 2 (HR2) plays a critical role in viral entry. Moreover, HR2 is both the target for novel antiviral therapies and, as an isolated peptide, presents a potential antiviral therapeutic. The structure of HR2, as determined by NMR spectroscopy in the presence of the co-solvent trifluoroethanol (TFE), is a trimer of parallel helices, whereas the structure of HR2, as determined by X-ray crystallography, is a tetramer of anti-parallel helices. In this work, we added a nitroxide spin label to the N-terminal region of HR2 and used paramagnetic relaxation enhancement to assess the orientation of the HR2 helices under different solution conditions. We find that the relaxation effects are consistent with an orientation corresponding to a trimer of parallel helices in both the presence and absence of TFE. This work suggests that the different orientation and oligomerization states observed by NMR and X-ray are due to the 11 additional residues present at the N-terminus of the NMR construct.
DOI: 10.1002/pro.736
PubMed: 21922588
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: Pour aller vers cette notice dans l'étape Curation :001472
Links to Exploration step
pubmed:21922588Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">SARS-CoV heptad repeat 2 is a trimer of parallel helices.</title><author><name sortKey="Celigoy, Jessica" sort="Celigoy, Jessica" uniqKey="Celigoy J" first="Jessica" last="Celigoy">Jessica Celigoy</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry & Molecular Genetics, University of Illinois at Chicago, Chicago, Illinois 60607, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry & Molecular Genetics, University of Illinois at Chicago, Chicago, Illinois 60607</wicri:regionArea></affiliation></author><author><name sortKey="Ramirez, Benjamin" sort="Ramirez, Benjamin" uniqKey="Ramirez B" first="Benjamin" last="Ramirez">Benjamin Ramirez</name></author><author><name sortKey="Caffrey, Michael" sort="Caffrey, Michael" uniqKey="Caffrey M" first="Michael" last="Caffrey">Michael Caffrey</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2011">2011</date><idno type="RBID">pubmed:21922588</idno><idno type="pmid">21922588</idno><idno type="doi">10.1002/pro.736</idno><idno type="wicri:Area/PubMed/Corpus">001472</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001472</idno><idno type="wicri:Area/PubMed/Curation">001472</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001472</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">SARS-CoV heptad repeat 2 is a trimer of parallel helices.</title><author><name sortKey="Celigoy, Jessica" sort="Celigoy, Jessica" uniqKey="Celigoy J" first="Jessica" last="Celigoy">Jessica Celigoy</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry & Molecular Genetics, University of Illinois at Chicago, Chicago, Illinois 60607, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry & Molecular Genetics, University of Illinois at Chicago, Chicago, Illinois 60607</wicri:regionArea></affiliation></author><author><name sortKey="Ramirez, Benjamin" sort="Ramirez, Benjamin" uniqKey="Ramirez B" first="Benjamin" last="Ramirez">Benjamin Ramirez</name></author><author><name sortKey="Caffrey, Michael" sort="Caffrey, Michael" uniqKey="Caffrey M" first="Michael" last="Caffrey">Michael Caffrey</name></author></analytic><series><title level="j">Protein science : a publication of the Protein Society</title><idno type="eISSN">1469-896X</idno><imprint><date when="2011" type="published">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Models, Molecular</term><term>Nuclear Magnetic Resonance, Biomolecular</term><term>Protein Multimerization</term><term>Protein Structure, Secondary</term><term>SARS Virus (chemistry)</term><term>Severe Acute Respiratory Syndrome (virology)</term><term>Spin Labels</term><term>Viral Envelope Proteins (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Marqueurs de spin</term><term>Modèles moléculaires</term><term>Multimérisation de protéines</term><term>Protéines de l'enveloppe virale ()</term><term>Résonance magnétique nucléaire biomoléculaire</term><term>Structure secondaire des protéines</term><term>Syndrome respiratoire aigu sévère (virologie)</term><term>Virus du SRAS ()</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Spin Labels</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Syndrome respiratoire aigu sévère</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Models, Molecular</term><term>Nuclear Magnetic Resonance, Biomolecular</term><term>Protein Multimerization</term><term>Protein Structure, Secondary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Marqueurs de spin</term><term>Modèles moléculaires</term><term>Multimérisation de protéines</term><term>Protéines de l'enveloppe virale</term><term>Résonance magnétique nucléaire biomoléculaire</term><term>Structure secondaire des protéines</term><term>Virus du SRAS</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In severe acute respiratory syndrome coronavirus, the envelope heptad repeat 2 (HR2) plays a critical role in viral entry. Moreover, HR2 is both the target for novel antiviral therapies and, as an isolated peptide, presents a potential antiviral therapeutic. The structure of HR2, as determined by NMR spectroscopy in the presence of the co-solvent trifluoroethanol (TFE), is a trimer of parallel helices, whereas the structure of HR2, as determined by X-ray crystallography, is a tetramer of anti-parallel helices. In this work, we added a nitroxide spin label to the N-terminal region of HR2 and used paramagnetic relaxation enhancement to assess the orientation of the HR2 helices under different solution conditions. We find that the relaxation effects are consistent with an orientation corresponding to a trimer of parallel helices in both the presence and absence of TFE. This work suggests that the different orientation and oligomerization states observed by NMR and X-ray are due to the 11 additional residues present at the N-terminus of the NMR construct.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21922588</PMID><DateCompleted><Year>2012</Year><Month>02</Month><Day>29</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1469-896X</ISSN><JournalIssue CitedMedium="Internet"><Volume>20</Volume><Issue>12</Issue><PubDate><Year>2011</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Protein science : a publication of the Protein Society</Title><ISOAbbreviation>Protein Sci.</ISOAbbreviation></Journal><ArticleTitle>SARS-CoV heptad repeat 2 is a trimer of parallel helices.</ArticleTitle><Pagination><MedlinePgn>2125-9</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1002/pro.736</ELocationID><Abstract><AbstractText>In severe acute respiratory syndrome coronavirus, the envelope heptad repeat 2 (HR2) plays a critical role in viral entry. Moreover, HR2 is both the target for novel antiviral therapies and, as an isolated peptide, presents a potential antiviral therapeutic. The structure of HR2, as determined by NMR spectroscopy in the presence of the co-solvent trifluoroethanol (TFE), is a trimer of parallel helices, whereas the structure of HR2, as determined by X-ray crystallography, is a tetramer of anti-parallel helices. In this work, we added a nitroxide spin label to the N-terminal region of HR2 and used paramagnetic relaxation enhancement to assess the orientation of the HR2 helices under different solution conditions. We find that the relaxation effects are consistent with an orientation corresponding to a trimer of parallel helices in both the presence and absence of TFE. This work suggests that the different orientation and oligomerization states observed by NMR and X-ray are due to the 11 additional residues present at the N-terminus of the NMR construct.</AbstractText><CopyrightInformation>Copyright © 2011 The Protein Society.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Celigoy</LastName><ForeName>Jessica</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Department of Biochemistry & Molecular Genetics, University of Illinois at Chicago, Chicago, Illinois 60607, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ramirez</LastName><ForeName>Benjamin</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Caffrey</LastName><ForeName>Michael</ForeName><Initials>M</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2011</Year><Month>11</Month><Day>01</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Protein Sci</MedlineTA><NlmUniqueID>9211750</NlmUniqueID><ISSNLinking>0961-8368</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013113">Spin Labels</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014759">Viral Envelope Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019906" MajorTopicYN="Y">Nuclear Magnetic Resonance, Biomolecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055503" MajorTopicYN="N">Protein Multimerization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045169" MajorTopicYN="N">Severe Acute Respiratory Syndrome</DescriptorName><QualifierName UI="Q000821" MajorTopicYN="N">virology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013113" MajorTopicYN="N">Spin Labels</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014759" MajorTopicYN="N">Viral Envelope Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2011</Year><Month>08</Month><Day>08</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2011</Year><Month>09</Month><Day>08</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2011</Year><Month>9</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2011</Year><Month>9</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2012</Year><Month>3</Month><Day>1</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">21922588</ArticleId><ArticleId IdType="doi">10.1002/pro.736</ArticleId><ArticleId IdType="pmc">PMC3302656</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>J Biomol NMR. 1995 Nov;6(3):277-93</Citation><ArticleIdList><ArticleId IdType="pubmed">8520220</ArticleId></ArticleIdList></Reference><Reference><Citation>FEBS Lett. 1988 Mar 14;229(2):317-24</Citation><ArticleIdList><ArticleId IdType="pubmed">3345845</ArticleId></ArticleIdList></Reference><Reference><Citation>Protein Sci. 1996 Jun;5(6):1067-80</Citation><ArticleIdList><ArticleId IdType="pubmed">8762138</ArticleId></ArticleIdList></Reference><Reference><Citation>Protein Sci. 1997 Nov;6(11):2359-64</Citation><ArticleIdList><ArticleId IdType="pubmed">9385638</ArticleId></ArticleIdList></Reference><Reference><Citation>J Magn Reson. 1997 Jan;124(1):154-64</Citation><ArticleIdList><ArticleId IdType="pubmed">9424305</ArticleId></ArticleIdList></Reference><Reference><Citation>Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):905-21</Citation><ArticleIdList><ArticleId IdType="pubmed">9757107</ArticleId></ArticleIdList></Reference><Reference><Citation>Q Rev Biophys. 1998 Aug;31(3):297-355</Citation><ArticleIdList><ArticleId IdType="pubmed">10384688</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2004 Nov 19;279(47):49414-9</Citation><ArticleIdList><ArticleId IdType="pubmed">15345712</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2004 Dec 28;101(52):17958-63</Citation><ArticleIdList><ArticleId IdType="pubmed">15604146</ArticleId></ArticleIdList></Reference><Reference><Citation>Virology. 2005 May 10;335(2):276-85</Citation><ArticleIdList><ArticleId IdType="pubmed">15840526</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2005 Aug 16;102(33):11876-81</Citation><ArticleIdList><ArticleId IdType="pubmed">16081529</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2006 Apr 28;281(17):11965-71</Citation><ArticleIdList><ArticleId IdType="pubmed">16507566</ArticleId></ArticleIdList></Reference><Reference><Citation>Structure. 2006 May;14(5):889-99</Citation><ArticleIdList><ArticleId IdType="pubmed">16698550</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2008 Jul 1;47(26):6802-8</Citation><ArticleIdList><ArticleId IdType="pubmed">18540634</ArticleId></ArticleIdList></Reference><Reference><Citation>J Magn Reson. 2009 Dec;201(2):218-21</Citation><ArticleIdList><ArticleId IdType="pubmed">19819173</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Biol. 2009 Dec 11;394(4):600-5</Citation><ArticleIdList><ArticleId IdType="pubmed">19853613</ArticleId></ArticleIdList></Reference><Reference><Citation>Trends Microbiol. 2011 Apr;19(4):191-7</Citation><ArticleIdList><ArticleId IdType="pubmed">21377881</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochem Biophys Res Commun. 2011 Sep 2;412(3):483-6</Citation><ArticleIdList><ArticleId IdType="pubmed">21835164</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2000 May 9;39(18):5355-65</Citation><ArticleIdList><ArticleId IdType="pubmed">10820006</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2003 Jun 13;278(24):21837-44</Citation><ArticleIdList><ArticleId IdType="pubmed">12672815</ArticleId></ArticleIdList></Reference><Reference><Citation>Nature. 2003 Nov 27;426(6965):450-4</Citation><ArticleIdList><ArticleId IdType="pubmed">14647384</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2004 Feb 24;43(7):1847-53</Citation><ArticleIdList><ArticleId IdType="pubmed">14967025</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Rev Drug Discov. 2004 Mar;3(3):215-25</Citation><ArticleIdList><ArticleId IdType="pubmed">15031735</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2004 Mar 23;101(12):4240-5</Citation><ArticleIdList><ArticleId IdType="pubmed">15010527</ArticleId></ArticleIdList></Reference><Reference><Citation>Lancet. 2004 Mar 20;363(9413):938-47</Citation><ArticleIdList><ArticleId IdType="pubmed">15043961</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2004 May 14;279(20):20836-49</Citation><ArticleIdList><ArticleId IdType="pubmed">14996844</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60</Citation><ArticleIdList><ArticleId IdType="pubmed">15150417</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Graph. 1996 Feb;14(1):51-5, 29-32</Citation><ArticleIdList><ArticleId IdType="pubmed">8744573</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/SrasV1/Data/PubMed/Curation
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001472 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Curation/biblio.hfd -nk 001472 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= SrasV1
|flux= PubMed
|étape= Curation
|type= RBID
|clé= pubmed:21922588
|texte= SARS-CoV heptad repeat 2 is a trimer of parallel helices.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Curation/RBID.i -Sk "pubmed:21922588" \
| HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Curation/biblio.hfd \
| NlmPubMed2Wicri -a SrasV1
| This area was generated with Dilib version V0.6.33. |  |