About: Structure of the SARS-Unique Domain C From the Bat Coronavirus HKU4

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An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Structure of the SARS-Unique Domain C From the Bat Coronavirus HKU4
Creator	Tan, Xuan Johnson, Margaret Hammond, Robert Catt, Justin De Silva, Ivon Staup, Andrew
Source	Medline; PMC
abstract	Coronaviruses (CoVs) that cause infections such as severe acute respiratory syndrome (SARS) and Middle East respiratory syndrome phylogenetically originate from bat CoVs. The coronaviral nonstructural protein 3 (nsp3) has been implicated in viral replication, polyprotein cleavage, and host immune interference. We report the structure of the C domain from the SARS-Unique Domain of bat CoV HKU4. The protein has a frataxin fold, consisting of 5 antiparallel β strands packed against 2 α helices. Bioinformatics analyses and nuclear magnetic resonance experiments were conducted to investigate the function of HKU4 C. The results showed that HKU4 C engages in protein-protein interactions with the nearby M domain of nsp3. The HKU4 C residues involved in protein-protein interactions are conserved in group 2c CoVs, indicating a conserved function.
has issue date	2019-05-27(xsd:dateTime)
bibo:doi	10.1177/1934578x19849202
bibo:pmid	32395093
has license	cc-by-nc
sha1sum (hex)	2bfcdf5569f14eacd54b0ea1593a8158bc1ee5d1
schema:url	https://doi.org/10.1177/1934578x19849202
resource representing a document's title	Structure of the SARS-Unique Domain C From the Bat Coronavirus HKU4
has PubMed Central identifier	PMC7206560
has PubMed identifier	32395093
schema:publication	Nat Prod Commun
resource representing a document's body	covid:2bfcdf5569f14eacd54b0ea1593a8158bc1ee5d1#body_text
is schema:about of	named entity 'NEARBY' named entity 'MIDDLE EAST RESPIRATORY SYNDROME ' named entity 'REPORT' named entity 'COVS' named entity 'Bioinformatics' named entity 'Coronaviruses' named entity 'protein' named entity 'SARS' named entity 'SARS' named entity 'antiparallel β strands' named entity 'severe acute respiratory syndrome' named entity 'nsp3' named entity 'Natural Product' named entity 'Biomedical Applications' named entity 'NMR' named entity 'heteronuclear single quantum coherence' named entity 'N-terminal' named entity 'tertiary structures' named entity 'RMSD' named entity 'codon' named entity 'conserved region' named entity 'alanine' named entity 'antiparallel β strands' named entity 'conserved regions' named entity 'NOESY' named entity 'CoV' named entity 'distance matrix' named entity 'secondary structure prediction' named entity 'protein-protein binding' named entity 'amino acid residues' named entity 'nucleocapsid protein' named entity 'sulfur' named entity 'variable region' named entity 'MERS CoV' named entity 'CoV' named entity 'p53' named entity 'protein' named entity 'protein-protein interactions' named entity 'tertiary structure' named entity 'SARS' named entity 'α helix' named entity 'host cell' named entity 'nsp' named entity 'conserved residues' named entity 'severe acute respiratory syndrome' named entity 'nsp' named entity 'functional site' named entity 'size-exclusion chromatography' named entity 'Switzerland' named entity 'MERS' named entity 'functional site' named entity 'protein' named entity 'α helix' named entity 'protein-protein interactions' named entity 'binding site' named entity 'HSQC' named entity 'previously identified' named entity 'calcium ions' named entity 'bat' named entity 'nuclear Overhauser effect' named entity 'COFACTOR' named entity '2.0' named entity 'chemical shift' named entity 'MHV' named entity 'protein' named entity 'acetate ion' named entity 'MHV' named entity 'United Kingdom' named entity '6xHis' named entity 'betacoronaviruses' named entity 'protein' named entity 'E. coli' named entity 'protein' named entity 'protein' named entity 'MHV' named entity 'folded protein'

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