Structure of the N-terminal RNA-binding domain of the SARS CoV nucleocapsid protein.
Identifieur interne : 002D95 ( PubMed/Curation ); précédent : 002D94; suivant : 002D96Structure of the N-terminal RNA-binding domain of the SARS CoV nucleocapsid protein.
Auteurs : Qiulong Huang [États-Unis] ; Liping Yu ; Andrew M. Petros ; Angelo Gunasekera ; Zhihong Liu ; Nan Xu ; Philip Hajduk ; Jamey Mack ; Stephen W. Fesik ; Edward T. OlejniczakSource :
- Biochemistry [ 0006-2960 ] ; 2004.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Nucleocapsid Proteins.
- chemical , metabolism : RNA.
- chemical : Ligands.
- chemistry : SARS Virus.
- Animals, Binding Sites, Humans, Models, Molecular, Molecular Sequence Data, Molecular Structure, Nuclear Magnetic Resonance, Biomolecular, Protein Folding, Protein Structure, Tertiary.
Abstract
The severe acute respiratory syndrome (SARS) virus belongs to the Coronaviridea family of viruses. Its virion encodes several proteins including a replicase and four structural proteins. Here we describe the three-dimensional structure of the N-terminal domain of the SARS coronavirus (CoV) nucleocapsid protein. The protein consists of a five-stranded beta sheet with a folding topology distinct from other RNA-binding proteins. Single-stranded RNAs bind to the protein surface at the junction between a flexible, positively charged beta hairpin and the core structure. NMR-based screening was used to identify low molecular weight compounds that bind to this site.
DOI: 10.1021/bi036155b
PubMed: 15147189
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Petros</name></author><author><name sortKey="Gunasekera, Angelo" sort="Gunasekera, Angelo" uniqKey="Gunasekera A" first="Angelo" last="Gunasekera">Angelo Gunasekera</name></author><author><name sortKey="Liu, Zhihong" sort="Liu, Zhihong" uniqKey="Liu Z" first="Zhihong" last="Liu">Zhihong Liu</name></author><author><name sortKey="Xu, Nan" sort="Xu, Nan" uniqKey="Xu N" first="Nan" last="Xu">Nan Xu</name></author><author><name sortKey="Hajduk, Philip" sort="Hajduk, Philip" uniqKey="Hajduk P" first="Philip" last="Hajduk">Philip Hajduk</name></author><author><name sortKey="Mack, Jamey" sort="Mack, Jamey" uniqKey="Mack J" first="Jamey" last="Mack">Jamey Mack</name></author><author><name sortKey="Fesik, Stephen W" sort="Fesik, Stephen W" uniqKey="Fesik S" first="Stephen W" last="Fesik">Stephen W. Fesik</name></author><author><name sortKey="Olejniczak, Edward T" sort="Olejniczak, Edward T" uniqKey="Olejniczak E" first="Edward T" last="Olejniczak">Edward T. 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Its virion encodes several proteins including a replicase and four structural proteins. Here we describe the three-dimensional structure of the N-terminal domain of the SARS coronavirus (CoV) nucleocapsid protein. The protein consists of a five-stranded beta sheet with a folding topology distinct from other RNA-binding proteins. Single-stranded RNAs bind to the protein surface at the junction between a flexible, positively charged beta hairpin and the core structure. NMR-based screening was used to identify low molecular weight compounds that bind to this site.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15147189</PMID><DateCompleted><Year>2004</Year><Month>08</Month><Day>23</Day></DateCompleted><DateRevised><Year>2004</Year><Month>11</Month><Day>17</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-2960</ISSN><JournalIssue CitedMedium="Print"><Volume>43</Volume><Issue>20</Issue><PubDate><Year>2004</Year><Month>May</Month><Day>25</Day></PubDate></JournalIssue><Title>Biochemistry</Title><ISOAbbreviation>Biochemistry</ISOAbbreviation></Journal><ArticleTitle>Structure of the N-terminal RNA-binding domain of the SARS CoV nucleocapsid protein.</ArticleTitle><Pagination><MedlinePgn>6059-63</MedlinePgn></Pagination><Abstract><AbstractText>The severe acute respiratory syndrome (SARS) virus belongs to the Coronaviridea family of viruses. Its virion encodes several proteins including a replicase and four structural proteins. Here we describe the three-dimensional structure of the N-terminal domain of the SARS coronavirus (CoV) nucleocapsid protein. The protein consists of a five-stranded beta sheet with a folding topology distinct from other RNA-binding proteins. Single-stranded RNAs bind to the protein surface at the junction between a flexible, positively charged beta hairpin and the core structure. NMR-based screening was used to identify low molecular weight compounds that bind to this site.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Huang</LastName><ForeName>Qiulong</ForeName><Initials>Q</Initials><AffiliationInfo><Affiliation>Global Pharmaceutical Discovery Division, Abbott Laboratories, Abbott Park, Illinois 60064-6098, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yu</LastName><ForeName>Liping</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Petros</LastName><ForeName>Andrew M</ForeName><Initials>AM</Initials></Author><Author ValidYN="Y"><LastName>Gunasekera</LastName><ForeName>Angelo</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Zhihong</ForeName><Initials>Z</Initials></Author><Author ValidYN="Y"><LastName>Xu</LastName><ForeName>Nan</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Hajduk</LastName><ForeName>Philip</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Mack</LastName><ForeName>Jamey</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Fesik</LastName><ForeName>Stephen W</ForeName><Initials>SW</Initials></Author><Author ValidYN="Y"><LastName>Olejniczak</LastName><ForeName>Edward T</ForeName><Initials>ET</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>PDB</DataBankName><AccessionNumberList><AccessionNumber>1SSK</AccessionNumber></AccessionNumberList></DataBank><DataBank><DataBankName>SWISSPROT</DataBankName><AccessionNumberList><AccessionNumber>P59595</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochemistry</MedlineTA><NlmUniqueID>0370623</NlmUniqueID><ISSNLinking>0006-2960</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008024">Ligands</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019590">Nucleocapsid Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>63231-63-0</RegistryNumber><NameOfSubstance UI="D012313">RNA</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008024" MajorTopicYN="N">Ligands</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015394" MajorTopicYN="N">Molecular Structure</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019906" MajorTopicYN="N">Nuclear Magnetic Resonance, Biomolecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019590" MajorTopicYN="N">Nucleocapsid Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017510" MajorTopicYN="N">Protein Folding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="Y">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012313" MajorTopicYN="N">RNA</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2004</Year><Month>5</Month><Day>19</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2004</Year><Month>8</Month><Day>24</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2004</Year><Month>5</Month><Day>19</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">15147189</ArticleId><ArticleId IdType="doi">10.1021/bi036155b</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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