About: Structural Basis of Inhibition Specificities of 3C and 3C-like Proteases by Zinc-coordinating and Peptidomimetic Compounds

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About: Structural Basis of Inhibition Specificities of 3C and 3C-like Proteases by Zinc-coordinating and Peptidomimetic Compounds Goto Sponge NotDistinct Permalink

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

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Structural Basis of Inhibition Specificities of 3C and 3C-like Proteases by Zinc-coordinating and Peptidomimetic Compounds
Creator	Kuo, Chih-Jung Liang, Po-Huang Shih, Shin-Ru Chang, Shih-Cheng Chen, Hua-Chien Chen, Shu-Jen Hsu, Min-Feng Hsu, Ming-Chu Ko, Tzu-Ping Lee, Cheng-Chung Tsui, Yao-Chen Yang, Syaulan Wang, -J
topic	covid:701d74c9df8d02f3be36f77cb8784ef524cce3e6#this
source	Medline; PMC
abstract	Human coxsackievirus (CV) belongs to the picornavirus family, which consists of over 200 medically relevant viruses. In picornavirus, a chymotrypsin-like protease (3C(pro)) is required for viral replication by processing the polyproteins, and thus it is regarded as an antiviral drug target. A 3C-like protease (3CL(pro)) also exists in human coronaviruses (CoV) such as 229E and the one causing severe acute respiratory syndrome (SARS). To combat SARS, we previously had developed peptidomimetic and zinc-coordinating inhibitors of 3CL(pro). As shown in the present study, some of these compounds were also found to be active against 3C(pro) of CV strain B3 (CVB3). Several crystal structures of 3C(pro) from CVB3 and 3CL(pro) from CoV-229E and SARS-CoV in complex with the inhibitors were solved. The zinc-coordinating inhibitor is tetrahedrally coordinated to the His(40)-Cys(147) catalytic dyad of CVB3 3C(pro). The presence of specific binding pockets for the residues of peptidomimetic inhibitors explains the binding specificity. Our results provide a structural basis for inhibitor optimization and development of potential drugs for antiviral therapies.
has issue date	2009-01-14(xsd:dateTime)
bibo:doi	10.1074/jbc.m807947200
bibo:pmid	19144641
has license	bronze-oa
sha1sum (hex)	701d74c9df8d02f3be36f77cb8784ef524cce3e6
schema:url	https://doi.org/10.1074/jbc.m807947200
resource representing a document's title	Structural Basis of Inhibition Specificities of 3C and 3C-like Proteases by Zinc-coordinating and Peptidomimetic Compounds
has PubMed Central identifier	PMC2658058
has PubMed identifier	19144641
schema:publication	Journal of Biological Chemistry
resource representing a document's body	covid:701d74c9df8d02f3be36f77cb8784ef524cce3e6#body_text
is http://vocab.deri.ie/void#inDataset of	proxy:http/ns.inria.fr/covid19/701d74c9df8d02f3be36f77cb8784ef524cce3e6
is schema:about of	named entity 'STRUCTURAL' named entity 'SPECIFICITIES' named entity 'development' named entity 'consists' named entity 'coordinated' named entity 'tetrahedrally' named entity 'severe acute respiratory syndrome (SARS)' named entity 'Proteases' named entity 'LIKE' named entity 'PROTEASES' named entity 'ZINC' named entity 'RELEVANT' named entity 'SARS' named entity 'CHYMOTRYPSIN-LIKE PROTEASE' named entity 'SPECIFIC' named entity 'PRESENT' named entity '200' named entity 'PROTEASE' named entity 'STUDY' named entity 'BASIS' named entity '229E' named entity 'CVB3' named entity 'COORDINATING' named entity 'OPTIMIZATION' named entity 'ACTIVE' named entity 'VIRAL REPLICATION' named entity 'ZINC' named entity 'STRUCTURES' named entity 'THERAPIES' named entity 'RESULTS' named entity 'BINDING' named entity 'PEPTIDOMIMETIC' named entity 'INHIBITION' named entity 'OUR' named entity 'PRO' named entity 'CORONAVIRUSES' named entity 'SEVERE ACUTE RESPIRATORY SYNDROME' named entity 'ANTIVIRAL DRUG' named entity 'COORDINATED' named entity 'CATALYTIC' named entity 'POTENTIAL' named entity 'BASIS' named entity 'CYS' named entity 'COMPLEX' named entity 'STRAIN' named entity 'CAUSING' named entity 'HUMAN COXSACKIEVIRUS' named entity 'CRYSTAL' named entity 'COMBAT' named entity 'DRUGS' named entity 'PREVIOUSLY' named entity 'INHIBITOR' named entity 'PICORNAVIRUS' named entity 'VIRUSES' named entity 'DEVELOPMENT' named entity 'DRUG TARGET' named entity 'REQUIRED' named entity 'FAMILY' named entity 'THESE' named entity 'COORDINATING' named entity 'SARS-COV' named entity 'BINDING SPECIFICITY' named entity 'PROCESSING' named entity 'HUMAN' named entity 'PROVIDE' named entity 'LIKE' named entity 'INHIBITORS'

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