About: Structural basis for dimerization and RNA binding of avian infectious bronchitis virus nsp9

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About: Structural basis for dimerization and RNA binding of avian infectious bronchitis virus nsp9 Goto Sponge NotDistinct Permalink

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	Structural basis for dimerization and RNA binding of avian infectious bronchitis virus nsp9
Creator	Yang, Haitao Zhou, Ming Chen, Cheng Li, Huiyan Su, Dan Yang, Cheng Dou, Yanshu Hu, Honggang Hu, Tingting Li, Yulei Lu, Deren Singh, Namit Zhang, Rundong Zhong, Zhihui Zong, Qi
Source	Medline; PMC
abstract	The potential for infection by coronaviruses (CoVs) has become a serious concern with the recent emergence of Middle East respiratory syndrome and severe acute respiratory syndrome (SARS) in the human population. CoVs encode two large polyproteins, which are then processed into 15–16 nonstructural proteins (nsps) that make significant contributions to viral replication and transcription by assembling the RNA replicase complex. Among them, nsp9 plays an essential role in viral replication by forming a homodimer that binds single‐stranded RNA. Thus, disrupting nsp9 dimerization is a potential anti‐CoV therapy. However, different nsp9 dimer forms have been reported for alpha‐ and beta‐CoVs, and no structural information is available for gamma‐CoVs. Here we determined the crystal structure of nsp9 from the avian infectious bronchitis virus (IBV), a representative gamma‐CoV that affects the economy of the poultry industry because it can infect domestic fowl. IBV nsp9 forms a homodimer via interactions across a hydrophobic interface, which consists of two parallel alpha helices near the carboxy terminus of the protein. The IBV nsp9 dimer resembles that of SARS‐CoV nsp9, indicating that this type of dimerization is conserved among all CoVs. This makes disruption of the dimeric interface an excellent strategy for developing anti‐CoV therapies. To facilitate this effort, we characterized the roles of six conserved residues on this interface using site‐directed mutagenesis and a multitude of biochemical and biophysical methods. We found that three residues are critical for nsp9 dimerization and its abitlity to bind RNA.
has issue date	2017-04-20(xsd:dateTime)
bibo:doi	10.1002/pro.3150
bibo:pmid	28257598
has license	bronze-oa
sha1sum (hex)	39d57801c57e1abf6a5f5e9e05f9834a1dd7ee90
schema:url	https://doi.org/10.1002/pro.3150
resource representing a document's title	Structural basis for dimerization and RNA binding of avian infectious bronchitis virus nsp9
has PubMed Central identifier	PMC5405427
has PubMed identifier	28257598
schema:publication	Protein Science
resource representing a document's body	covid:39d57801c57e1abf6a5f5e9e05f9834a1dd7ee90#body_text
is schema:about of	named entity 'dimer' named entity 'SARS-CoV' named entity 'code' named entity 'Accession' named entity 'RNA' named entity 'infection' named entity 'RNA' named entity 'binds' named entity 'economy' named entity 'therapy' named entity 'nonstructural proteins' named entity 'dimerization' named entity 'carboxy terminus' named entity 'poultry industry' named entity 'dimerization' named entity 'dimer' named entity 'alpha helices' named entity 'nonstructural proteins' named entity 'crystal structure' named entity 'viral replication' named entity 'hydrophobic' named entity 'RCSB Protein Data Bank' named entity 'protein' named entity 'avian infectious bronchitis virus' named entity 'homodimer' named entity 'IBV' named entity 'papain' named entity 'phylogenetic tree' named entity 'a-helices' named entity 'viral infection' named entity 'SDS-PAGE' named entity 'wild-type' named entity 'disulfide bridge' named entity 'conserved residues' named entity 'protomer' named entity 'nucleic acids' named entity 'dimer' named entity 'pairwise sequence alignment' named entity 'space group' named entity 'single-stranded' named entity 'Mutation' named entity 'virus' named entity 'homodimer' named entity 'RNA' named entity 'wild-type' named entity 'genome' named entity 'IBV' named entity 'dimerization' named entity 'GE Healthcare' named entity 'dimer' named entity 'An-50' named entity 'C-terminal' named entity 'RNA' named entity 'protein' named entity 'a-helical' named entity 'unit cell' named entity 'IBV' named entity 'IBV' named entity 'Electrospray ionization mass spectrometry' named entity 'RNA' named entity 'IBV' named entity 'Wild-type' named entity 'conserved residues' named entity 'I432' named entity 'polyprotein' named entity 'Rigaku' named entity 'SPR'

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