Search results for "Scissile bond"

showing 3 items of 3 documents

The C-terminal region of human plasma fetuin-B is dispensable for the raised-elephant-trunk mechanism of inhibition of astacin metallopeptidases

2019

© The Author(s) 2019.

0301 basic medicineProteasesProtein Conformationlcsh:MedicineAstacoideaCrystallography X-RayCleavage (embryo)Protein Structure SecondaryArticleMice03 medical and health sciencesScissile bondHydrolaseAnimalsHumansAmino Acid Sequencelcsh:ScienceProtein secondary structureX-ray crystallographyBinding SitesMultidisciplinary030102 biochemistry & molecular biologyChemistrylcsh:RMetalloendopeptidasesProteasesFetuinFetuin-BCell biologyZincFertility030104 developmental biologyProteolysisMetalloproteaseslcsh:QAstacinLinkerScientific Reports
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A Microscopic Description of SARS-CoV-2 Main Protease Inhibition with Michael Acceptors. Strategies for Improving Inhibitors Design

2020

The irreversible inhibition of the main protease of SARS-CoV-2 by a Michael acceptor known as N3 has been investigated using multiscale methods. The noncovalent enzyme–inhibitor complex was simulated using classical molecular dynamics techniques and the pose of the inhibitor in the active site was compared to that of the natural substrate, a peptide containing the Gln–Ser scissile bond. The formation of the covalent enzyme–inhibitor complex was then simulated using hybrid QM/MM free energy methods. After binding, the reaction mechanism was found to be composed of two steps: (i) the activation of the catalytic dyad (Cys145 and His41) to form an ion pair and (ii) a Michael addition where the …

0303 health sciencesReaction mechanismProteasebiologyStereochemistryChemistrymedicine.medical_treatmenteducationActive siteSubstrate (chemistry)General Chemistry010402 general chemistry01 natural sciences0104 chemical sciencesQM/MM03 medical and health sciencesChemistryMolecular dynamicsScissile bondCovalent bondmedicinebiology.proteinMichael reaction030304 developmental biology
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Substrate determinants for cleavage in cis and in trans by the hepatitis C virus NS3 proteinase

1995

Processing of the hepatitis C virus polyprotein is accomplished by a series of cotranslational and posttranslational cleavages mediated by host cell signalases and two virally encoded proteinases. Of these the NS3 proteinase is essential for processing at the NS3/4A, NS4A/4B, NS4B/5A, and NS5A/5B junctions. Processing between NS3 and NS4A occurs in cis, implying an intramolecular reaction mechanism, whereas cleavage at the other sites can also be mediated in trans. Sequence analysis of the amino termini of mature cleavage products and comparisons of amino acid residues around the scissile bonds of various hepatitis C virus isolates identified amino acid residues which might contribute to su…

Cleavage factorvirusesMolecular Sequence DataImmunologyHepacivirusCleavage and polyadenylation specificity factorViral Nonstructural ProteinsBiologyCleavage (embryo)MicrobiologySubstrate SpecificityScissile bondVirologyHumansAmino Acid SequenceAmino AcidsPeptide sequencechemistry.chemical_classificationNS3Cleavage stimulation factorHydrolysisSerine Endopeptidasesbiochemical phenomena metabolism and nutritionAmino acidchemistryBiochemistryMutagenesisInsect ScienceProtein Processing Post-TranslationalRNA HelicasesHeLa CellsResearch ArticleJournal of Virology
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