Recent development of 3C and 3CL protease inhibitors for anti-coronavirus and anti-picornavirus drug discovery.
Identifieur interne : 002059 ( Main/Exploration ); précédent : 002058; suivant : 002060Recent development of 3C and 3CL protease inhibitors for anti-coronavirus and anti-picornavirus drug discovery.
Auteurs : R. Ramajayam [Taïwan] ; Kian-Pin Tan ; Po-Huang LiangSource :
- Biochemical Society transactions [ 1470-8752 ] ; 2011.
Descripteurs français
- KwdFr :
- Cysteine endopeptidases (métabolisme), Cysteine endopeptidases (ultrastructure), Découverte de médicament, Humains, Infections à Picornaviridae (traitement médicamenteux), Inhibiteurs de protéases (), Inhibiteurs de protéases (pharmacologie), Inhibiteurs de protéases (usage thérapeutique), Picornaviridae (), Picornaviridae (enzymologie), Picornaviridae (physiologie), Protéines virales (antagonistes et inhibiteurs), Protéines virales (métabolisme), Protéines virales (ultrastructure), Réplication virale, Structure moléculaire.
- MESH :
- antagonistes et inhibiteurs : Protéines virales.
- enzymologie : Picornaviridae.
- métabolisme : Cysteine endopeptidases, Protéines virales.
- pharmacologie : Inhibiteurs de protéases.
- physiologie : Picornaviridae.
- traitement médicamenteux : Infections à Picornaviridae.
- ultrastructure : Cysteine endopeptidases, Protéines virales.
- usage thérapeutique : Inhibiteurs de protéases.
- Découverte de médicament, Humains, Inhibiteurs de protéases, Picornaviridae, Réplication virale, Structure moléculaire.
English descriptors
- KwdEn :
- Cysteine Endopeptidases (metabolism), Cysteine Endopeptidases (ultrastructure), Drug Discovery, Humans, Molecular Structure, Picornaviridae (drug effects), Picornaviridae (enzymology), Picornaviridae (physiology), Picornaviridae Infections (drug therapy), Protease Inhibitors (chemistry), Protease Inhibitors (pharmacology), Protease Inhibitors (therapeutic use), Viral Proteins (antagonists & inhibitors), Viral Proteins (metabolism), Viral Proteins (ultrastructure), Virus Replication.
- MESH :
- chemical , antagonists & inhibitors : Viral Proteins.
- chemical , chemistry : Protease Inhibitors.
- chemical , metabolism : Cysteine Endopeptidases, Viral Proteins.
- chemical , pharmacology : Protease Inhibitors.
- chemical , therapeutic use : Protease Inhibitors.
- chemical , ultrastructure : Cysteine Endopeptidases, Viral Proteins.
- drug effects : Picornaviridae.
- drug therapy : Picornaviridae Infections.
- enzymology : Picornaviridae.
- physiology : Picornaviridae.
- Drug Discovery, Humans, Molecular Structure, Virus Replication.
Abstract
SARS-CoV (severe acute respiratory syndrome-associated coronavirus) caused infection of ~8000 people and death of ~800 patients around the world during the 2003 outbreak. In addition, picornaviruses such as enterovirus, coxsackievirus and rhinovirus also can cause life-threatening diseases. Replication of picornaviruses and coronaviruses requires 3Cpro (3C protease) and 3CLpro (3C-like protease) respectively, which are structurally analogous with chymotrypsin-fold, but the former is a monomer and the latter is dimeric due to an extra third domain for dimerization. Subtle structural differences in the S2 and S3 pockets of these proteases make inhibitors selective, but some dual inhibitors have been discovered. Our findings as summarized in the present review provide new potential anti-coronavirus and anti-picornavirus therapeutic agents and a clue to convert 3CLpro inhibitors into 3Cpro inhibitors and vice versa.
DOI: 10.1042/BST0391371
PubMed: 21936817
Affiliations:
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Le document en format XML
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moléculaire</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">SARS-CoV (severe acute respiratory syndrome-associated coronavirus) caused infection of ~8000 people and death of ~800 patients around the world during the 2003 outbreak. In addition, picornaviruses such as enterovirus, coxsackievirus and rhinovirus also can cause life-threatening diseases. Replication of picornaviruses and coronaviruses requires 3Cpro (3C protease) and 3CLpro (3C-like protease) respectively, which are structurally analogous with chymotrypsin-fold, but the former is a monomer and the latter is dimeric due to an extra third domain for dimerization. Subtle structural differences in the S2 and S3 pockets of these proteases make inhibitors selective, but some dual inhibitors have been discovered. Our findings as summarized in the present review provide new potential anti-coronavirus and anti-picornavirus therapeutic agents and a clue to convert 3CLpro inhibitors into 3Cpro inhibitors and vice versa.</div></front></TEI><affiliations><list><country><li>Taïwan</li></country></list><tree><noCountry><name sortKey="Liang, Po Huang" sort="Liang, Po Huang" uniqKey="Liang P" first="Po-Huang" last="Liang">Po-Huang Liang</name><name sortKey="Tan, Kian Pin" sort="Tan, Kian Pin" uniqKey="Tan K" first="Kian-Pin" last="Tan">Kian-Pin Tan</name></noCountry><country name="Taïwan"><noRegion><name sortKey="Ramajayam, R" sort="Ramajayam, R" uniqKey="Ramajayam R" first="R" last="Ramajayam">R. Ramajayam</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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