About: The N-terminal octapeptide acts as a dimerization inhibitor of SARS coronavirus 3C-like proteinase

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About: The N-terminal octapeptide acts as a dimerization inhibitor of SARS coronavirus 3C-like proteinase 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
has title	The N-terminal octapeptide acts as a dimerization inhibitor of SARS coronavirus 3C-like proteinase
Creator	Liu, Ying Wei, Ping Xi, Dong Tan, Lei Chen, Hao Ma, Liang Fan, Keqiang Lai, Luhua Li, Chunmei Cao, Aoneng Huang, Changkang
Source	Elsevier; Medline; PMC
abstract	Abstract The 3C-like proteinase of severe acute respiratory syndrome (SARS) coronavirus has been proposed to be a key target for structural-based drug design against SARS. Accurate determination of the dimer dissociation constant and the role of the N-finger (residues 1–7) will provide more insights into the enzyme catalytic mechanism of SARS 3CL proteinase. The dimer dissociation constant of the wild-type protein was determined to be 14.0μM by analytical ultracentrifugation method. The N-finger fragment of the enzyme plays an important role in enzyme dimerization as shown in the crystal structure. Key residues in the N-finger have been studied by site-directed mutagenesis, enzyme assay, and analytical ultracentrifugation. A single mutation of M6A was found to be critical to maintain the dimer structure of the enzyme. The N-terminal octapeptide N8 and its mutants were also synthesized and tested for their potency as dimerization inhibitors. Peptide cleavage assay confirms that peptide N8 is a dimerization inhibitor with a K i of 2.20mM. The comparison of the inhibitory activities of N8 and its mutants indicates that the hydrophobic interaction of Met-6 and the electrostatic interaction of Arg-4 contribute most for inhibitor binding. This study describes the first example of inhibitors targeting the dimeric interface of SARS 3CL proteinase, providing a novel strategy for drug design against SARS and other coronaviruses.
has issue date	2006-01-20(xsd:dateTime)
bibo:doi	10.1016/j.bbrc.2005.11.102
bibo:pmid	16329994
has license	els-covid
sha1sum (hex)	9da556907fdb754d24163b6647246dd16ae2a281
schema:url	https://doi.org/10.1016/j.bbrc.2005.11.102
resource representing a document's title	The N-terminal octapeptide acts as a dimerization inhibitor of SARS coronavirus 3C-like proteinase
has PubMed Central identifier	PMC7092940
has PubMed identifier	16329994
schema:publication	Biochemical and Biophysical Research Communications
resource representing a document's body	covid:9da556907fdb754d24163b6647246dd16ae2a281#body_text
is schema:about of	named entity 'site-directed mutagenesis' named entity 'target' named entity 'structure' named entity 'inhibitory' named entity 'analytical ultracentrifugation' named entity 'hydrophobic interaction' named entity 'residues' named entity 'study' named entity 'DETERMINATION' named entity 'CORONAVIRUSES' named entity 'PROTEIN ' named entity 'COMPARISON' named entity 'IS A' named entity 'SINGLE' named entity 'WILDTYPE' named entity 'PROTEINASE' named entity 'DRUG DESIGN' named entity 'SARS' named entity 'PROVIDE' named entity 'PEPTIDE' named entity 'CRYSTAL STRUCTURE' named entity 'ENZYME' named entity 'MET-' named entity 'PROPOSED' named entity 'CLEAVAGE ASSAY' named entity 'THEIR' named entity 'ROLE' named entity 'M6A' named entity 'INHIBITOR' named entity 'FINGER' named entity 'N-TERMINAL ' named entity 'INHIBITORS' named entity 'PROVIDING' named entity 'FRAGMENT OF' named entity 'STRUCTURE' named entity 'ARG-' named entity 'TARGET' named entity 'CORONAVIRUS' named entity 'INHIBITOR' named entity 'PROTEINASE' named entity 'DIMER' named entity 'SEVERE ACUTE RESPIRATORY SYNDROME' named entity '1-7' named entity 'SYNTHESIZED' named entity 'ACTS' named entity 'SARS CORONAVIRUS' named entity 'LIKE' named entity 'PLAYS' named entity 'NOVEL' named entity 'IMPORTANT' named entity 'FOUND' named entity 'DIMERIZATION' named entity 'HAVE' named entity 'BINDING' named entity 'ANALYTICAL ULTRACENTRIFUGATION' named entity 'METHOD' named entity 'ENZYME ASSAY' named entity 'MUTATION' named entity 'ACTIVITIES' named entity 'KEY' named entity 'STUDY' named entity 'MUTANTS' named entity 'DISSOCIATION CONSTANT' named entity 'DIMERIZATION' named entity 'HYDROPHOBIC INTERACTION' named entity 'LIKE' named entity 'ITS' named entity 'CATALYTIC MECHANISM' named entity 'TESTED FOR' named entity 'TO MAINTAIN' named entity 'CONFIRMS'

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