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Article: The nsp9 Replicase Protein of SARS-Coronavirus, Structure and Functional Insights

TitleThe nsp9 Replicase Protein of SARS-Coronavirus, Structure and Functional Insights
Authors
Issue Date2004
PublisherCell Press. The Journal's web site is located at http://www.elsevier.com/locate/str
Citation
Structure, 2004, v. 12 n. 2, p. 341-353 How to Cite?
AbstractAs part of a high-throughput structural analysis of SARS-coronavirus (SARS-CoV) proteins, we have solved the structure of the non-structural protein 9 (nsp9). This protein, encoded by ORF1a, has no designated function but is most likely involved with viral RNA synthesis. The protein comprises a single β-barrel with a fold previously unseen in single domain proteins. The fold superficially resembles an OB-fold with a C-terminal extension and is related to both of the two subdomains of the SARS-CoV 3C-like protease (which belongs to the serine protease superfamily). nsp9 has, presumably, evolved from a protease. The crystal structure suggests that the protein is dimeric. This is confirmed by analytical ultracentrifugation and dynamic light scattering. We show that nsp9 binds RNA and interacts with nsp8, activities that may be essential for its function(s).
Persistent Identifierhttp://hdl.handle.net/10722/78999
ISSN
2015 Impact Factor: 5.237
2015 SCImago Journal Rankings: 4.770
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorSutton, Gen_HK
dc.contributor.authorFry, Een_HK
dc.contributor.authorCarter, Len_HK
dc.contributor.authorSainsbury, Sen_HK
dc.contributor.authorWalter, Ten_HK
dc.contributor.authorNettleship, Jen_HK
dc.contributor.authorBerrow, Nen_HK
dc.contributor.authorOwens, Ren_HK
dc.contributor.authorGilbert, Ren_HK
dc.contributor.authorDavidson, Aen_HK
dc.contributor.authorSiddell, Sen_HK
dc.contributor.authorPoon, LLMen_HK
dc.contributor.authorDiprose, Jen_HK
dc.contributor.authorAlderton, Den_HK
dc.contributor.authorWalsh, Men_HK
dc.contributor.authorGrimes, JMen_HK
dc.contributor.authorStuart, DIen_HK
dc.date.accessioned2010-09-06T07:49:22Z-
dc.date.available2010-09-06T07:49:22Z-
dc.date.issued2004en_HK
dc.identifier.citationStructure, 2004, v. 12 n. 2, p. 341-353en_HK
dc.identifier.issn0969-2126en_HK
dc.identifier.urihttp://hdl.handle.net/10722/78999-
dc.description.abstractAs part of a high-throughput structural analysis of SARS-coronavirus (SARS-CoV) proteins, we have solved the structure of the non-structural protein 9 (nsp9). This protein, encoded by ORF1a, has no designated function but is most likely involved with viral RNA synthesis. The protein comprises a single β-barrel with a fold previously unseen in single domain proteins. The fold superficially resembles an OB-fold with a C-terminal extension and is related to both of the two subdomains of the SARS-CoV 3C-like protease (which belongs to the serine protease superfamily). nsp9 has, presumably, evolved from a protease. The crystal structure suggests that the protein is dimeric. This is confirmed by analytical ultracentrifugation and dynamic light scattering. We show that nsp9 binds RNA and interacts with nsp8, activities that may be essential for its function(s).en_HK
dc.languageengen_HK
dc.publisherCell Press. The Journal's web site is located at http://www.elsevier.com/locate/stren_HK
dc.relation.ispartofStructureen_HK
dc.titleThe nsp9 Replicase Protein of SARS-Coronavirus, Structure and Functional Insightsen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0969-2126&volume=12&spage=341&epage=353&date=2004&atitle=The+nsp9+replicase+protein+of+SARS-coronavirus,+structure+and+functional+insightsen_HK
dc.identifier.emailPoon, LLM: llmpoon@hkucc.hku.hken_HK
dc.identifier.authorityPoon, LLM=rp00484en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/S0969-2126(04)00026-7en_HK
dc.identifier.pmid14962394-
dc.identifier.scopuseid_2-s2.0-10744222104en_HK
dc.identifier.hkuros88004en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-10744222104&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume12en_HK
dc.identifier.issue2en_HK
dc.identifier.spage341en_HK
dc.identifier.epage353en_HK
dc.identifier.isiWOS:000221430100021-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridSutton, G=7202240603en_HK
dc.identifier.scopusauthoridFry, E=7102301301en_HK
dc.identifier.scopusauthoridCarter, L=7201576485en_HK
dc.identifier.scopusauthoridSainsbury, S=8835866400en_HK
dc.identifier.scopusauthoridWalter, T=34573834600en_HK
dc.identifier.scopusauthoridNettleship, J=6508017512en_HK
dc.identifier.scopusauthoridBerrow, N=6701388728en_HK
dc.identifier.scopusauthoridOwens, R=7201383882en_HK
dc.identifier.scopusauthoridGilbert, R=9736375100en_HK
dc.identifier.scopusauthoridDavidson, A=7402001807en_HK
dc.identifier.scopusauthoridSiddell, S=7005260816en_HK
dc.identifier.scopusauthoridPoon, LLM=7005441747en_HK
dc.identifier.scopusauthoridDiprose, J=6603082306en_HK
dc.identifier.scopusauthoridAlderton, D=36808002000en_HK
dc.identifier.scopusauthoridWalsh, M=7402337622en_HK
dc.identifier.scopusauthoridGrimes, JM=7101923612en_HK
dc.identifier.scopusauthoridStuart, DI=7201612248en_HK

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