About: Essential covalent linkage between the chymotrypsin-like domain and the extra domain of the SARS-CoV main protease

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About: Essential covalent linkage between the chymotrypsin-like domain and the extra domain of the SARS-CoV main protease 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
has title	Essential covalent linkage between the chymotrypsin-like domain and the extra domain of the SARS-CoV main protease
Creator	Chang, Gu-Gang Chang, Hui-Ping Chang, Wei-Hsin Liang, Jin-Yi Lin, Long-Liu Tsai, Ying
Source	Medline; PMC
abstract	The main protease of the coronavirus causing severe acute respiratory syndrome performs proteolytic processing of the viral polyproteins. The active form of the enzyme is a homodimer with each subunit consisting of three structural domains. Domains I and II, hosting the complete catalytic machinery, constitute the N-terminal chymotrypsin-like folding scaffold and connect to the extra C-terminal domain III by a long loop. Previously, the domain III-truncated enzyme was demonstrated to fold independently into an intact chymotrypsin-like fold, but it showed no enzyme activity. To further delineate the structure–function relationships of the domain III and the long loop, we generated some truncated and mutated M(pro) forms bearing various combinations of the loop with other structural parts of the enzyme. Their conformational and association properties were investigated in detail. Far-ultraviolet circular dichroism (CD) measurements revealed that these fragments could fold independently. The secondary, tertiary and quaternary structures of these mixtures were monitored by CD, fluorescence spectroscopy and analytical ultracentrifugation. However, no enzyme activity was observed for any mutant or mixtures. These observations indicate that the covalent linkage between the chymotrypsin like and the extra domain is essential for enzymatic activity of the main coronavirus protease and for the integrity of its quaternary structure.
has issue date	2010-08-28(xsd:dateTime)
bibo:doi	10.1093/jb/mvq071
bibo:pmid	20587646
has license	no-cc
sha1sum (hex)	56b1fe4f2caed17c950576a545a762d8adc4473a
schema:url	https://doi.org/10.1093/jb/mvq071
resource representing a document's title	Essential covalent linkage between the chymotrypsin-like domain and the extra domain of the SARS-CoV main protease
has PubMed Central identifier	PMC7110190
has PubMed identifier	20587646
schema:publication	J Biochem
resource representing a document's body	covid:56b1fe4f2caed17c950576a545a762d8adc4473a#body_text
is schema:about of	named entity 'PROTEASE' named entity 'Domains' named entity 'fold' named entity 'N-terminal' named entity 'secondary' named entity 'causing' named entity 'folding' named entity 'enzyme' named entity 'independently' named entity 'DOMAIN' named entity 'LIKE' named entity 'OBSERVED' named entity 'C-TERMINAL' named entity 'RELATIONSHIPS' named entity 'MIXTURES' named entity 'MUTANT' named entity 'SUBUNIT' named entity 'CAUSING' named entity 'FORM' named entity 'THESE' named entity 'CONNECT' named entity 'REVEALED' named entity 'FORMS' named entity 'MEASUREMENTS' named entity 'SEVERE ACUTE RESPIRATORY SYNDROME' named entity 'VIRAL' named entity 'HOMODIMER' named entity 'PROTEASE' named entity 'ENZYME ACTIVITY' named entity 'DELINEATE' named entity 'LIKE' named entity 'COVALENT LINKAGE' named entity 'ULTRAVIOLET' named entity 'HOSTING' named entity 'PROPERTIES' named entity 'FLUORESCENCE SPECTROSCOPY' named entity 'N-TERMINAL ' named entity 'STRUCTURES' named entity 'STRUCTURAL' named entity 'ENZYMATIC ACTIVITY' named entity 'MAIN' named entity 'CHYMOTRYPSIN' named entity 'CATALYTIC' named entity 'PROTEOLYTIC PROCESSING' named entity 'GENERATED' named entity 'COVALENT LINKAGE' named entity 'SARS-COV' named entity 'III' named entity 'VARIOUS COMBINATIONS' named entity 'INVESTIGATED' named entity 'PRO' named entity 'CORONAVIRUS' named entity 'LONG' named entity 'IS A' named entity 'EXTRA' named entity 'LOOP' named entity 'MAIN' named entity 'ESSENTIAL' named entity 'DOMAIN' named entity 'ITS' named entity 'FAR' named entity 'FOLD' named entity 'FRAGMENTS' named entity 'ASSOCIATION' named entity 'ANALYTICAL ULTRACENTRIFUGATION' named entity 'MONITORED' named entity 'FOLDING' named entity 'PREVIOUSLY' named entity 'PARTS' named entity 'SECONDARY' named entity 'MACHINERY' named entity 'EXTRA' named entity 'MUTATED' named entity 'ESSENTIAL' named entity 'SCAFFOLD' named entity 'QUATERNARY STRUCTURE'

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