Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra α‐helical domain

Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra α‐helical domain

Source :

• The EMBO Journal [ 0261-4189 ] ; 2002-07-01.

Descripteurs français

• KwdFr :
  • Alignement de séquences, Chymotrypsine (), Conformation des protéines, Cristallographie aux rayons X, Cysteine endopeptidases (), Cysteine endopeptidases (génétique), Dimérisation, Données de séquences moléculaires, Liaison aux protéines, Modèles moléculaires, Mutagenèse, Pliage des protéines, Protéines de fusion recombinantes (), Similitude de séquences d'acides aminés, Sites de fixation, Structure tertiaire des protéines, Séquence d'acides aminés, Virus de la gastroentérite transmissible (enzymologie), Virus de la gastroentérite transmissible (génétique).
• MESH :
  • enzymologie : Virus de la gastroentérite transmissible.
  • génétique : Cysteine endopeptidases, Virus de la gastroentérite transmissible.
  • Alignement de séquences, Chymotrypsine, Conformation des protéines, Cristallographie aux rayons X, Cysteine endopeptidases, Dimérisation, Données de séquences moléculaires, Liaison aux protéines, Modèles moléculaires, Mutagenèse, Pliage des protéines, Protéines de fusion recombinantes, Similitude de séquences d'acides aminés, Sites de fixation, Structure tertiaire des protéines, Séquence d'acides aminés.

English descriptors

• KwdEn :
  • Amino Acid Sequence, Binding Sites, Chymotrypsin (chemistry), Crystallography, X-Ray, Cysteine Endopeptidases (chemistry), Cysteine Endopeptidases (genetics), Dimerization, Models, Molecular, Molecular Sequence Data, Mutagenesis, Protein Binding, Protein Conformation, Protein Folding, Protein Structure, Tertiary, Recombinant Fusion Proteins (chemistry), Sequence Alignment, Sequence Homology, Amino Acid, Transmissible gastroenteritis virus (enzymology), Transmissible gastroenteritis virus (genetics).
• MESH :
  • chemical , chemistry : Chymotrypsin, Cysteine Endopeptidases, Recombinant Fusion Proteins.
  • chemical , genetics : Cysteine Endopeptidases.
  • enzymology : Transmissible gastroenteritis virus.
  • genetics : Transmissible gastroenteritis virus.
• Teeft :
  • 3cpro, Aaaggatccttatgacatgacattagtaccttccaattg atggcacagcctagtggtcttgta, Acta crystallogr, Active site, Active site cleft, Amino, Amino Acid Sequence, Amino acid residues, Ammonium sulfate, Asymmetric, Asymmetric unit, Bergmann, Binding Sites, Biol, Catalytic, Catalytic centre, Catalytic site, Catalytic triad, Chymotrypsin, Cleavage, Cleavage sites, Coding sequence, Coronavirus, Coronavirus mpro, Crystal structure, Crystal structures, Crystallization medium, Crystallogr, Crystallography, X-Ray, Cysteine, Cysteine proteinases, Data collection, Data sets, Diffraction beamline, Diffraction data, Dimer, Dimerization, Domain, Electron density, Electron density maps, Embl outstation, Enzymatic activities, Experimental data, Febs lett, Gene product, Glutamine, Glutamine side chain, Hcov, Hegyi, Helix, Histidine, Histidine residues, Human coronavirus, Human rhinovirus, Hydrogen bond, Hydrogen bonds, Hydrophobic, Hydrophobic pocket, Hydrophobic residues, Hydroxyl group, Imidazole side chain, Loop region, Main chain, Main chain amides, Models, Molecular, Molecular Sequence Data, Molecular modelling, Molecule, Monomer, Mpro, Mpro residues, Mpro structure, Mpro substrates, Mutagenesis, Mutant, Mutant proteins, Mutational analysis, Mutual arrangement, Natl acad, Neutral state, Nucleic acids, Other members, Other monomers, Outer wall, Oxyanion hole, Peak wavelengths, Peptide, Peptide inhibitors, Phase problem, Picornavirus, Proper orientation, Protease, Protein Binding, Protein Conformation, Protein Folding, Protein Structure, Tertiary, Protein structures, Proteinase, Proteinase activity, Proteolytic, Proteolytic activities, Proteolytic activity, Proteolytic processing, Proteolytic products, Quality indicator, Recombinant proteins, Remote wavelengths, Replicase polyproteins, Replicative polyproteins, Residue, Salt bridge, Scissile bond, Secondary structure elements, Sequence Alignment, Sequence Homology, Amino Acid, Serine, Serine proteases, Serine proteinases, Side chain, Side chains, Solvent content, Structural information, Structure determination, Structure factors, Subsite, Substrate binding, Sulfur atom, Tgev, Tgev mpro, Tgev mpro autoprocessing site, Tgev mpro crystal structure, Third member, Transmissible gastroenteritis virus, Unit cell dimensions, Viral, Viral cysteine proteinase, Virol, Virology, Water molecule, Water molecules, Ziebuhr.

Abstract

• https://api.istex.fr/ark:/67375/WNG-MSHVSPN0-B/fulltext.pdf
• http://www.ncbi.nlm.nih.gov/pmc/articles/PMC126080

Affiliations:

• Allemagne
• Bavière, District de Basse-Franconie
• Wurtzbourg

Links toward previous steps (curation, corpus...)

• to stream Istex, to step Corpus: 000645
• to stream Istex, to step Curation: 000625
• to stream Istex, to step Checkpoint: 000326
• to stream Pmc, to step Corpus: 000220
• to stream Pmc, to step Curation: 000220
• to stream Pmc, to step Checkpoint: 000712
• to stream PubMed, to step Corpus: 000721
• to stream PubMed, to step Curation: 000721
• to stream PubMed, to step Checkpoint: 000712
• to stream Ncbi, to step Merge: 000020
• to stream Ncbi, to step Curation: 000020
• to stream Ncbi, to step Checkpoint: 000020
• to stream Main, to step Merge: 001127
• to stream Main, to step Curation: 001115

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