About: (1)H, (13)C and (15)N resonance assignments of SARS-CoV main protease N-terminal domain

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About: (1)H, (13)C and (15)N resonance assignments of SARS-CoV main protease N-terminal domain Goto Sponge NotDistinct Permalink

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

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	(1)H, (13)C and (15)N resonance assignments of SARS-CoV main protease N-terminal domain
Creator	Zhang, Shengnan Zhong, Nan Bin Xia, Jin Changwen, Ren Xiaobai, •
Source	Medline; PMC
abstract	The main protease (M(pro)) of severe acute respiratory syndrome coronavirus (SARS-CoV) plays an essential role in the extensive proteolytic processing of the viral polyproteins (pp1a and pp1ab), and it is an important target for anti-SARS drug development. SARS-CoV M(pro) is composed of a catalytic N-terminal domain and an α-helical C-terminal domain linked by a long loop. Even though the N-terminal domain of SARS-CoV M(pro) adopts a similar chymotrypsin-like fold as that of piconavirus 3C protease, the extra C-terminal domain is required for SARS-CoV M(pro) to be enzymatically active. Here, we reported the NMR assignments of the SARS-CoV M(pro) N-terminal domain alone, which are essential for its solution structure determination.
has issue date	2010-12-23(xsd:dateTime)
bibo:doi	10.1007/s12104-010-9287-9
bibo:pmid	21181312
has license	no-cc
sha1sum (hex)	c593e36a0fadce9f72d823ad42d4f52cdd6c6d04
schema:url	https://doi.org/10.1007/s12104-010-9287-9
resource representing a document's title	(1)H, (13)C and (15)N resonance assignments of SARS-CoV main protease N-terminal domain
has PubMed Central identifier	PMC7091140
has PubMed identifier	21181312
schema:publication	Biomol NMR Assign
resource representing a document's body	covid:c593e36a0fadce9f72d823ad42d4f52cdd6c6d04#body_text
is schema:about of	named entity 'N-TERMINAL ' named entity 'SARS-CoV' named entity 'solution' named entity 'severe acute respiratory syndrome coronavirus' named entity 'structure determination' named entity 'polyproteins' named entity 'N-terminal domain' named entity 'assignments' named entity 'EXTENSIVE' named entity 'PROTEOLYTIC PROCESSING' named entity 'CHYMOTRYPSIN' named entity 'HERE' named entity 'ROLE' named entity 'STRUCTURE DETERMINATION' named entity 'FOLD' named entity 'ACTIVE' named entity 'CATALYTIC' named entity 'LIKE' named entity 'PRO' named entity 'NMR' named entity 'DOMAIN' named entity 'PROTEASE N' named entity 'MAIN' named entity 'RESONANCE' named entity 'SARS-COV' named entity 'SARS' named entity 'ESSENTIAL' named entity 'PLAYS' named entity 'VIRAL' named entity 'SOLUTION' named entity 'HELICAL' named entity 'DOMAIN' named entity 'SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS' named entity 'COMPOSED OF' named entity 'REQUIRED' named entity 'TARGET' named entity 'SARS-COV' named entity 'IMPORTANT' named entity 'MAIN' named entity 'N-TERMINAL ' named entity 'REPORTED' named entity 'POLYPROTEINS' named entity 'SIMILAR' named entity 'EXTRA' named entity 'C-TERMINAL' named entity 'LONG' named entity 'DRUG DEVELOPMENT' named entity 'PROTEASE' named entity 'ITS' named entity 'LOOP' covid:arg/c593e36a0fadce9f72d823ad42d4f52cdd6c6d04 named entity 'essential' named entity 'enzymatically active' named entity 'essential' named entity 'loop' named entity 'protease' named entity 'fold' named entity 'SARS-CoV' named entity 'a-helical' named entity 'SARS-CoV' named entity 'protease' named entity 'drug development' named entity 'SARS-CoV' named entity 'N-terminal domain' named entity 'SARS-CoV' named entity 'CBCA' named entity 'SARS-CoV' named entity 'SARS-CoV' named entity 'chemical shift' named entity 'C-terminal domain' named entity 'protease' named entity 'NMR experiments' named entity 'high-quality' named entity 'N-terminal domain' named entity 'potassium phosphate' named entity 'protease' named entity 'Arginine'

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