About: Solution Structure of the C-terminal Dimerization Domain of SARS Coronavirus Nucleocapsid Protein Solved by the SAIL-NMR Method

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About: Solution Structure of the C-terminal Dimerization Domain of SARS Coronavirus Nucleocapsid Protein Solved by the SAIL-NMR Method Goto Sponge NotDistinct Permalink

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

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Solution Structure of the C-terminal Dimerization Domain of SARS Coronavirus Nucleocapsid Protein Solved by the SAIL-NMR Method
Creator	Hsu, Yen-Lan Chang, Chung-Ke Huang, Tai-Huang Chang, Yuan-Hsiang Güntert, Peter Ikeya, Teppei Kainosho, Masatsune Takeda, Mitsuhiro
source	Elsevier; Medline; PMC
abstract	Abstract The C-terminal domain (CTD) of the severe acute respiratory syndrome coronavirus (SARS-CoV) nucleocapsid protein (NP) contains a potential RNA-binding region in its N-terminal portion and also serves as a dimerization domain by forming a homodimer with a molecular mass of 28 kDa. So far, the structure determination of the SARS-CoV NP CTD in solution has been impeded by the poor quality of NMR spectra, especially for aromatic resonances. We have recently developed the stereo-array isotope labeling (SAIL) method to overcome the size problem of NMR structure determination by utilizing a protein exclusively composed of stereo- and regio-specifically isotope-labeled amino acids. Here, we employed the SAIL method to determine the high-quality solution structure of the SARS-CoV NP CTD by NMR. The SAIL protein yielded less crowded and better resolved spectra than uniform 13C and 15N labeling, and enabled the homodimeric solution structure of this protein to be determined. The NMR structure is almost identical with the previously solved crystal structure, except for a disordered putative RNA-binding domain at the N-terminus. Studies of the chemical shift perturbations caused by the binding of single-stranded DNA and mutational analyses have identified the disordered region at the N-termini as the prime site for nucleic acid binding. In addition, residues in the β-sheet region also showed significant perturbations. Mapping of the locations of these residues onto the helical model observed in the crystal revealed that these two regions are parts of the interior lining of the positively charged helical groove, supporting the hypothesis that the helical oligomer may form in solution.
has issue date	2008-07-18(xsd:dateTime)
bibo:doi	10.1016/j.jmb.2007.11.093
bibo:pmid	18561946
has license	els-covid
sha1sum (hex)	58c67994f47dc6c8b552cff7de2892719259ec52
schema:url	https://doi.org/10.1016/j.jmb.2007.11.093
resource representing a document's title	Solution Structure of the C-terminal Dimerization Domain of SARS Coronavirus Nucleocapsid Protein Solved by the SAIL-NMR Method
has PubMed Central identifier	PMC7094413
has PubMed identifier	18561946
schema:publication	Journal of Molecular Biology
resource representing a document's body	covid:58c67994f47dc6c8b552cff7de2892719259ec52#body_text
is schema:about of	named entity 'NUCLEOCAPSID PROTEIN' named entity 'METHOD' named entity 'OLIGOMER' named entity 'POOR QUALITY' named entity 'DOMAIN' named entity 'POTENTIAL' named entity 'REVEALED' named entity 'SAIL' named entity 'CRYSTAL' named entity 'EXCEPT FOR' named entity 'SIZE' named entity 'ISOTOPE LABELING' named entity 'STEREO' named entity 'OBSERVED' named entity 'MODEL' named entity 'CONTAINS' named entity 'HERE' named entity 'QUALITY' named entity 'RNA' named entity 'FAR' named entity 'ENABLED' named entity 'PROTEIN ' named entity 'C-TERMINAL' named entity 'DOMAIN' named entity 'NMR' named entity 'NUCLEOCAPSID PROTEIN' named entity 'LABELED' covid:arg/58c67994f47dc6c8b552cff7de2892719259ec52 named entity 'KDA' named entity 'HYPOTHESIS' named entity 'HIGH' named entity 'COMPOSED OF' named entity 'N-TERMINAL ' named entity 'HOMODIMER' named entity 'PRIME' named entity 'STRUCTURE DETERMINATION' named entity 'RECENTLY' named entity 'SHEET' named entity 'BETTER' named entity 'LINING' named entity 'OVERCOME' named entity 'PROTEIN ' named entity 'NUCLEIC ACID BINDING' named entity 'TERMINAL PORTION' named entity 'IMPEDED' named entity 'PARTS' named entity 'HELICAL' named entity 'ISOTOPE' named entity 'MAPPING' named entity 'METHOD' named entity 'DISORDERED REGION' named entity 'IDENTICAL' named entity 'EMPLOYED' named entity 'STRUCTURE' named entity 'SARS CORONAVIRUS' named entity 'DIMERIZATION' named entity 'SOLUTION' named entity 'BINDING' named entity 'UNIFORM' named entity 'A PROTEIN' named entity 'CROWDED' named entity 'SIGNIFICANT' named entity 'BINDING REGION' named entity 'SUPPORTING' named entity 'THESE' named entity 'FORMING' named entity 'SAIL' named entity 'C-TERMINAL' named entity 'IDENTIFIED' named entity 'PREVIOUSLY' named entity 'GROOVE' named entity 'N-TERMINUS' named entity 'MOLECULAR MASS' named entity 'POSITIVELY CHARGED'

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