About: Crystal structure-based exploration of the important role of Arg106 in the RNA-binding domain of human coronavirus OC43 nucleocapsid protein

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About: Crystal structure-based exploration of the important role of Arg106 in the RNA-binding domain of human coronavirus OC43 nucleocapsid protein Goto Sponge NotDistinct Permalink

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

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Crystal structure-based exploration of the important role of Arg106 in the RNA-binding domain of human coronavirus OC43 nucleocapsid protein
Creator	Hou, Ming-Hon Zhao, Jincun Perlman, Stanley Chang, Yu-Ming Huang, Tai-Huang Lin, Shing-Yen Chen, I.-Jung Shen, Yo-Yu Yuann, Jeu-Ming
Source	Elsevier; Medline; PMC
abstract	Human coronavirus OC43 (HCoV-OC43) is a causative agent of the common cold. The nucleocapsid (N) protein, which is a major structural protein of CoVs, binds to the viral RNA genome to form the virion core and results in the formation of the ribonucleoprotein (RNP) complex. We have solved the crystal structure of the N-terminal domain of HCoV-OC43 N protein (N-NTD) (residues 58 to 195) to a resolution of 2.0Å. The HCoV-OC43 N-NTD is a single domain protein composed of a five-stranded β-sheet core and a long extended loop, similar to that observed in the structures of N-NTDs from other coronaviruses. The positively charged loop of the HCoV-OC43 N-NTD contains a structurally well-conserved positively charged residue, R106. To assess the role of R106 in RNA binding, we undertook a series of site-directed mutagenesis experiments and docking simulations to characterize the interaction between R106 and RNA. The results show that R106 plays an important role in the interaction between the N protein and RNA. In addition, we showed that, in cells transfected with plasmids that encoded the mutant (R106A) N protein and infected with virus, the level of the matrix protein gene was decreased by 7-fold compared to cells that were transfected with the wild-type N protein. This finding suggests that R106, by enhancing binding of the N protein to viral RNA plays a critical role in the viral replication. The results also indicate that the strength of N protein/RNA interactions is critical for HCoV-OC43 replication.
has issue date	2013-06-01(xsd:dateTime)
bibo:doi	10.1016/j.bbapap.2013.03.003
bibo:pmid	23501675
has license	bronze-oa
sha1sum (hex)	64b61cc66756c7a27c061f63d5f0e2788130cd03
schema:url	https://doi.org/10.1016/j.bbapap.2013.03.003
resource representing a document's title	Crystal structure-based exploration of the important role of Arg106 in the RNA-binding domain of human coronavirus OC43 nucleocapsid protein
has PubMed Central identifier	PMC3774783
has PubMed identifier	23501675
schema:publication	Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
resource representing a document's body	covid:64b61cc66756c7a27c061f63d5f0e2788130cd03#body_text
is schema:about of	named entity 'transfected' named entity 'long' named entity 'protein' named entity 'enhancing' named entity 'HCoV-OC43' named entity 'wild-type' named entity 'series' named entity 'structure-based' named entity 'BASED' named entity 'ENCODED' named entity 'BINDS' named entity 'FOLD' named entity 'N PROTEIN' named entity 'CELLS' named entity 'FORMATION' named entity 'SERIES' named entity 'RNA' named entity 'SINGLE' named entity 'NTD' named entity 'CORE' named entity 'DECREASED BY' named entity 'ADDITION' named entity 'OF SITE' named entity 'TO FORM' named entity 'INTERACTION' named entity 'MUTANT' named entity 'IMPORTANT' named entity 'RESULTS' named entity 'LEVEL' named entity 'LONG' named entity 'A MAJOR' named entity 'PLASMIDS' named entity 'RNA BINDING' named entity 'SITE-DIRECTED MUTAGENESIS' named entity 'PROTEIN GENE' named entity 'MATRIX PROTEIN' named entity 'REPLICATION' named entity 'RESIDUE' named entity 'ROLE' named entity 'HUMAN CORONAVIRUS OC43' named entity 'STRUCTURAL PROTEIN' named entity 'ENHANCING' named entity 'COMMON COLD' named entity 'EXPERIMENTS' named entity 'INTERACTIONS' named entity 'HCOV-OC43' named entity 'SIMILAR' named entity 'STRUCTURES' named entity 'VIRION' named entity 'IS A' named entity 'INFECTED' named entity 'RESOLUTION' named entity 'RIBONUCLEOPROTEIN' named entity 'COMPOSED OF' named entity 'SHEET' named entity 'OBSERVED' named entity 'DOMAIN' named entity 'DOMAIN' named entity 'IMPORTANT' named entity 'N-TERMINAL ' named entity 'CAUSATIVE AGENT' named entity 'COMPARED' named entity 'PLAYS' named entity 'VIRAL REPLICATION' named entity 'COMPLEX' named entity 'HUMAN CORONAVIRUS OC43' named entity 'NUCLEOCAPSID PROTEIN' named entity 'ROLE' named entity 'BINDING' named entity 'EXPLORATION' named entity 'LOOP' named entity 'ASSESS' named entity 'TO CHARACTERIZE'

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