About: The crystal structure of main protease from mouse hepatitis virus A59 in complex with an inhibitor

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About: The crystal structure of main protease from mouse hepatitis virus A59 in complex with an inhibitor 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	The crystal structure of main protease from mouse hepatitis virus A59 in complex with an inhibitor
Creator	Yang, Haitao Zhang, Lei Cui, Wen Chen, Cheng Chen, Xia Wang, Zefang Cui, Shanshan
Source	Elsevier; Medline; PMC
abstract	Abstract Mouse hepatitis virus A59 (MHV-A59) is a representative member of the genus betacoronavirus within the subfamily Coronavirinae, which infects the liver, brain and respiratory tract. Through different inoculation routes, MHV-A59 can provide animal models for encephalitis, hepatitis and pneumonia to explore viral life machinery and virus-host interactions. In viral replication, non-structural protein 5 (Nsp5), also termed main protease (Mpro), plays a dominant role in processing coronavirus-encoded polyproteins and is thus recognized as an ideal target of anti-coronavirus agents. However, no structure of the MHV-A59 Mpro has been reported, and molecular exploration of the catalysis mechanism remains hindered. Here, we solved the crystal structure of the MHV-A59 Mpro complexed with a Michael acceptor-based inhibitor, N3. Structural analysis revealed that the Cβ of the vinyl group of N3 covalently bound to C145 of the catalytic dyad of Mpro, which irreversibly inactivated cysteine protease activity. The lactam ring of the P1 side chain and the isobutyl group of the P2 side chain, which mimic the conserved residues at the same positions of the substrate, fit well into the S1 and S2 pockets. Through a comparative study with Mpro of other coronaviruses, we observed that the substrate-recognition pocket and enzyme inhibitory mechanism is highly conservative. Altogether, our study provided structural features of MHV-A59 Mpro and indicated that a Michael acceptor inhibitor is an ideal scaffold for antiviral drugs.
has issue date	2019-04-16(xsd:dateTime)
bibo:doi	10.1016/j.bbrc.2019.02.105
bibo:pmid	30833083
has license	els-covid
sha1sum (hex)	3e19dcc43686493e4e329e94f8da9518eb5d77e5
schema:url	https://doi.org/10.1016/j.bbrc.2019.02.105
resource representing a document's title	The crystal structure of main protease from mouse hepatitis virus A59 in complex with an inhibitor
has PubMed Central identifier	PMC7185540
has PubMed identifier	30833083
schema:publication	Biochemical and Biophysical Research Communications
resource representing a document's body	covid:3e19dcc43686493e4e329e94f8da9518eb5d77e5#body_text
is schema:about of	named entity 'PROTEASE' named entity 'viral replication' named entity 'inoculation' named entity 'enzyme' named entity 'machinery' named entity 'member' named entity 'pro' named entity 'IDEAL' named entity 'PRO' named entity 'VIRUS' named entity 'PROTEASE' named entity 'VIRAL REPLICATION' named entity 'ANTIVIRAL DRUGS' named entity 'MAIN' named entity 'HIGHLY' named entity 'MICHAEL' named entity 'PNEUMONIA' named entity 'SCAFFOLD' named entity 'STUDY' named entity 'REPRESENTATIVE' named entity 'ROUTES' named entity 'MOUSE HEPATITIS VIRUS' named entity 'DOMINANT' named entity 'MACHINERY' named entity 'NON-STRUCTURAL PROTEIN 5' named entity 'SUBSTRATE' named entity 'BRAIN' named entity 'RECOGNITION' named entity 'OBSERVED' named entity 'CRYSTAL STRUCTURE' named entity 'CORONAVIRUSES' named entity 'ANTI-CORONAVIRUS AGENTS' named entity 'A59' named entity 'INHIBITOR' named entity 'LACTAM RING' named entity 'GENUS BETACORONAVIRUS' named entity 'SIDE CHAIN' named entity 'FEATURES' named entity 'EXPLORATION' named entity 'ANIMAL MODELS ' named entity 'ROLE' named entity 'REVEALED' named entity 'RESPIRATORY TRACT' named entity 'INHIBITOR' named entity 'ENCODED' named entity 'POLYPROTEINS' named entity 'VINYL GROUP' named entity 'IS A' named entity 'COMPARATIVE STUDY' named entity 'VIRAL' named entity 'CORONAVIRUS' named entity 'TARGET' named entity 'ENCEPHALITIS' named entity 'MECHANISM' named entity 'DYAD' named entity 'LIVER' named entity 'CYSTEINE PROTEASE ACTIVITY' named entity 'ACCEPTOR' named entity 'MIMIC' named entity 'MOUSE HEPATITIS VIRUS' named entity 'COMPLEX' named entity 'HOST' named entity 'INACTIVATED' named entity 'REPORTED' named entity 'OUR' named entity 'HEPATITIS' named entity 'INFECTS' named entity 'STRUCTURAL' named entity 'SUBFAMILY CORONAVIRINAE' named entity 'CRYSTAL STRUCTURE' named entity 'CATALYSIS' named entity 'FIT' named entity 'DIFFERENT' named entity 'INOCULATION' named entity 'MOLECULAR'

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