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3.4.22.28: picornain 3C

This is an abbreviated version!
For detailed information about picornain 3C, go to the full flat file.

Word Map on EC 3.4.22.28

Reaction

Selective cleavage of Gln-/-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly =

Synonyms

3C protease, 3C protein, 3C proteinase, 3C-like protease, 3C-protease, 3CL, 3cLpro, 3CP, 3Cpro, 3Cpro protease, Avihepatovirus 3C protease, coxsackievirus 3C proteinase, cysteine proteinase 3C, DHAV 3C protease, enterovirus 3C protease, EV71 3Cpro, foot-and-mouth protease 3C, HAC 3C, HAV 3C protease, HAV 3Cpro, hepatitis A virus 3C proteinase, HRV 3C protease, HRV 3Cpro, HRV type-14 3C protease, HRV16 3C protease, Human rhinovirus 3C protease, human rhinovirus type-14 3C protease, nonstructural 3 protease, NS3 protease, NS6 protease, P3C, picornain 3C, picornain-3C, picornaviral 3C protease, picornavirus endopeptidase 3C, poliovirus protease 3C, poliovirus proteinase 3C, protease 3C, proteinase, foot-and-mouth-disease virus, 3C, proteinase, picornavirus, 3C, proteinase, poliovirus, 3C, proteinase, rhinovirus, 3C, rhinovirus 3C protease, rhinovirus protease 3C, SAT-type 3C protease, Senecavirus A 3C protease, SV3CP, SVA 3Cpro, tomato ringspot nepovirus 3C-related protease

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.28 picornain 3C

Crystallization

Crystallization on EC 3.4.22.28 - picornain 3C

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of AG7088 bound to serotype 2 rhinovirus 3C protease, hanging-drop vapor diffusion method
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crystal structure of inhibitors covalently bound to the enzyme, hanging drop vapor diffusion method
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high-resolution cocrystal structures for the inhibitors bound to the enzyme benzyloxycarbonyl-Leu-Phe-(N,N-dimethyl-glutaminyl), benzyloxycarbonyl-Leu-Phe-[methional sulfoxide] or benzyloxycarbonyl-Leu-Phe-(N-acetyl-aminoalaninal)
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high-resolution crystal structures of the EV71 3Cpro/rupintrivir complex is determined, showing that although rupintrivir interacts with EV71 3Cpro similarly to HRV 3Cpro, the C terminus of the inhibitor cannot accommodate the leaving-group pockets of EV71 3Cpro. EV71 3Cpro possesses a surface-recessive S2' pocket that is not present in HRV 3Cpro that contributes to the additional substrate binding affinity
in complex with rupintrivir, hanging drop vapor diffusion method, using 100 mM Tris-HCl pH 8.5, 25% (w/v) PEG 4000, 0.8 M lithium chloride
crystal structure of 3Cpro alone and in complex with the anti-HRV molecules compound (AG7404) and rupintrivir (AG7088) at resolutions of 1.9, 1.3, and 1.5 A is reported. This 20.2-kDa cysteine protease adopts a chymotrypsin-like fold with a catalytic triad, Cys147-His40-Glu71, located in the cleft between the two six-stranded barrels. The residues that form the inhibitor binding pockets are highly conserved among EV 3Cpros, which explains the broad activity of compounds developed initially against a specific virus
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sitting drop vapor diffusion method, using 0.07 M sodium acetate (pH 4.6), 5-15% (w/v) PEG 4000, and 10-30% (v/v) glycerol
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in complex with substrate APAKQLLNFD, sitting drop vapor diffusion method, using 40-42.5% (w/v)polyethylene glycol 400, 0.2 M LiSO4 and 0.1 M Tris (pH 8.0), and in complex with substrate APAKELLNFD, sitting drop vapor diffusion method, using 41-43% (w/v) polyethylene glycol 400, 0.2 M LiSO4 and 0.1 M Tris (pH 8.0)
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sitting drop vapour diffusion method with 16 to 22% polyethylene glycol 4000, 100 mM Tris HCl (pH 8.5), and 2 mM sodium acetate
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sitting drop vapour diffusion, at 1.9 A resolution
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sitting drop vapour diffusion, iterative crystal-screening strategy, at 1.9 A resolution
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recombinant detagged SAT1/N-g3Cpro(1-208), sitting drop vapour diffusion method, mixing of 100 nl of protein solution with 100 nl of reservoir solution, crystallization from mother liquor containing 15% w/v PEG 8000, 0.09 M Na-cacodylate pH 7.0, 0.27 M Ca-acetate, 0.01 M Tris, pH 8.5, and 0.08 M Na-thiocyanate, supplemented with 20% v/v glycerol, no crystals are obtained
recombinant detagged SAT2/G-g3Cpro(1-208), sitting drop vapour diffusion method, mixing of 100 nl of protein solution with 100 nl of reservoir solution, crystallization from mother liquor containing 15% w/v PEG 8000, 0.09 M Na-cacodylate pH 7.0, 0.27 M Ca-acetate, 0.01 M Tris, pH 8.5, and 0.08 M Na-thiocyanate, supplemented with 20% v/v glycerol, X-ray diffraction structure determination and analysis at 3.2 A resolution
recombinant detagged SAT2/Zg3Cpro(1-208), sitting drop vapour diffusion method, mixing of 100 nl of protein solution with 100 nl of reservoir solution, crystallization from mother liquor containing 15% w/v PEG-8000, 0.09 M Na-cacodylate pH 7.0, 0.27 M Ca-acetate, 0.01 M Tris, pH 8.5, and 0.08 M Na-thiocyanate, supplemented with 20% v/v glycerol, no crystals are obtained
double mutant C24S/C172A
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hanging drop vapor diffusion method at room temperature, to 1.5 A resolution
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in complex with inhibitors N-acetyl-L-leucyl-alanyl-alanyl-(N,N-dimethyl)-glutamine-fluoromethyl ketone, N-acetyl-L-leucyl-phenylalanyl-phenylalanyl-glutamate-fluoromethyl ketone, and N-acetyl-L-leucyl-alanyl-alanyl-(N,N-dimethyl)-glutamine-(1,4-dioxo-3,4-dihydro-1H-phthalazin-2-yl)methyl ketone
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purified recombinant enzyme bound to inhibitor GC376, X-ray diffraction structure determination and analysis at 1.6 A resolution, molecular replacement
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X-ray structure of the Southampton norovirus 3C protease (SV3CP) bound to an active site-directed peptide inhibitor which has been refined at 1.7 A resolution is described