About: Crystal Structures of the Main Peptidase from the SARS Coronavirus Inhibited by a Substrate-like Aza-peptide Epoxide

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About: Crystal Structures of the Main Peptidase from the SARS Coronavirus Inhibited by a Substrate-like Aza-peptide Epoxide 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	Crystal Structures of the Main Peptidase from the SARS Coronavirus Inhibited by a Substrate-like Aza-peptide Epoxide
Creator	Liu, Jie Huitema, Carly Lee, Ting-Wai Cherney, Maia Eltis, Lindsay James, Karen James, Michael Powers, James
Source	Elsevier; Medline; PMC
abstract	The main peptidase (Mpro) from the coronavirus (CoV) causing severe acute respiratory syndrome (SARS) is one of the most attractive molecular targets for the development of anti-SARS agents. We report the irreversible inhibition of SARS-CoV Mpro by an aza-peptide epoxide (APE; k inact/K i=1900(±400)M−1 s−1). The crystal structures of the Mpro:APE complex in the space groups C2 and P212121 revealed the formation of a covalent bond between the catalytic Cys145 Sγ atom of the peptidase and the epoxide C3 atom of the inhibitor, substantiating the mode of action of this class of cysteine-peptidase inhibitors. The aza-peptide component of APE binds in the substrate-binding regions of Mpro in a substrate-like manner, with excellent structural and chemical complementarity. In addition, the crystal structure of unbound Mpro in the space group C2 revealed that the “N-fingers” (N-terminal residues 1 to 7) of both protomers of Mpro are well defined and the substrate-binding regions of both protomers are in the catalytically competent conformation at the crystallization pH of 6.5, contrary to the previously determined crystal structures of unbound Mpro in the space group P21.
has issue date	2005-11-11(xsd:dateTime)
bibo:doi	10.1016/j.jmb.2005.09.004
bibo:pmid	16219322
has license	els-covid
sha1sum (hex)	da9b1de6f607c73b126717ebe9bac3d79885dabe
schema:url	https://doi.org/10.1016/j.jmb.2005.09.004
resource representing a document's title	Crystal Structures of the Main Peptidase from the SARS Coronavirus Inhibited by a Substrate-like Aza-peptide Epoxide
has PubMed Central identifier	PMC7094542
has PubMed identifier	16219322
schema:publication	Journal of Molecular Biology
resource representing a document's body	covid:da9b1de6f607c73b126717ebe9bac3d79885dabe#body_text
is schema:about of	named entity 'pro' named entity 'structural' named entity 'space group' named entity 'development' named entity 'agents' named entity 'Crystal' covid:arg/da9b1de6f607c73b126717ebe9bac3d79885dabe named entity 'crystal structures' named entity 'SARS-CoV' named entity 'manner' named entity 'conformation' named entity 'SARS-CoV' named entity 'atom' named entity 'epoxide' named entity 'crystal structures' named entity 'protomers' named entity 'SARS' named entity 'complementarity' named entity 'cysteine' named entity 'G400' named entity 'Crystal Structures' named entity 'Peptidase' named entity 'peptidase' named entity 'peptidase' named entity 'space group' named entity 'epoxide' named entity 'carbonyl' named entity '3.8' named entity 'crystal structure' named entity 'carbonyl' named entity 'amino group' named entity 'protomer' named entity 'liver' named entity 'a-helices' named entity 'side-chain' named entity 'epoxide' named entity 'Cbz' named entity 'protonation' named entity 'wavelength' named entity 'w/v' named entity 'X-ray diffraction' named entity 'sterically' named entity 'nucleophilic attack' named entity 'active site' named entity 'SARS-CoV' named entity 'protomer' named entity 'amino acid' named entity 'Cbz' named entity 'racemic mixture' named entity 'protomers' named entity 'protomer' named entity 'organic chemistry' named entity 'peptide' named entity 'deprotonation' named entity 'ethylene glycol' named entity 'papain' named entity 'Gly' named entity 'side-chains' named entity 'alkylating agents' named entity 'epoxide' named entity 'amino acid' named entity 'peptide' named entity 'cysteine peptidases' named entity 'crystal structures' named entity 'randomly selected' named entity 'peptidase' named entity 'kDa' named entity 'hydrogen bonds' named entity 'epoxide' named entity 'virus-cell interactions' named entity 'intracellular' named entity 'peptidase' named entity 'side-chain' named entity 'kDa'

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