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show all sequences of 3.4.21.90

The regulation of disassembly of alphavirus cores

Wengler, G.; Arch. Virol. 154, 381-390 (2009)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
additional information
the disassembly of cores is stimulated by increasing the concentration of NaCl, but neither octylglucoside nor low pH stimulates the reaction
Semliki forest virus
additional information
cores, which are resistant to trypsin at physiological salt concentrations, whereas become trypsin sensitive at elevated salt concentrations and under these conditions, the carboxy-terminal domain, beginning with position M(106) is released as a soluble protein. Use of endoproteinase LysC instead of trypsin allows a somewhat larger soluble carboxy-terminal domain beginning with Q(94). The disassembly of cores is stimulated by increasing the concentration of NaCl in the reaction, by the presence of octylglycoside, and by lowering the pH of the reaction to 6.0 and is not stimulated by the presence of NP 40
Sindbis virus
Application
Application
Commentary
Organism
drug development
alphavirus core protein is a target for antiviral chemotherapy
Chikungunya virus
drug development
alphavirus core protein is a target for antiviral chemotherapy
Semliki forest virus
drug development
alphavirus core protein is a target for antiviral chemotherapy
Sindbis virus
Crystallization (Commentary)
Crystallization (Commentary)
Organism
at 25 A resolution
Ross River virus
at 9 A resolution, the C-terminal domain folds into a trypsin-like protease structure
Semliki forest virus
at 9 A resolution, the carboxyterminal domain folds into a trypsin-like protease structure
Sindbis virus
Engineering
Protein Variants
Commentary
Organism
drug development
alphavirus core protein is a target for antiviral chemotherapy
Ross River virus
additional information
mutants containing deletions of residues P(105) to D(118) and M(111) to D(118) in the core protein are viable, but the specific infectivity of these viruses is about 10fold less than the infectivity of wild-type virus. After lysis of infected cells or virus particles, mutant core protein with deletion of residues Q(40) to R(118) behaves as a monomer, whereby the core is generated during virus particle formation by the collection of core protein molecules by the viral membrane proteins prior to and/or during assembly of the viral surface proteins into an icosahedral shell
Semliki forest virus
additional information
mutant containing a deletion of residues K(97) to M(106), wild-type-like cores are assembled in the cytoplasm, and particle formation is largely unaffected, but 26S subgenomic viral RNA, which is not incorporated into wild-type particles, is efficiently packaged into cores and virus particles. Mutations in the linker region and in neighbouring regions of the core protein have no effect on disassembly of viral cores during virus entry
Sindbis virus
Inhibitors
Inhibitors
Commentary
Organism
Structure
additional information
the carboxy-terminal amino acid residues of the core protein remain associated to the active site after cleavage and thereby inactivate the enzyme
Semliki forest virus
additional information
the carboxy-terminal amino acid residues of the core protein remain associated to the active site after cleavage and thereby inactivate the enzyme
Sindbis virus
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
additional information
in the host, the core protein is transferred to ribosomes, the ribosome bound core protein is distributed throughout the cytoplasm, whereas the genome RNA remains associated with vacuolar membranes
Semliki forest virus
-
-
Organism
Organism
UniProt
Commentary
Textmining
Chikungunya virus
-
-
-
Ross River virus
-
-
-
Semliki forest virus
-
-
-
Sindbis virus
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
additional information
the active site of the protease releases the core protein from the growing polyprotein containing all structural proteins during translation. A short linker sequence connects the basic domain to the protease domain. In the Sindbis virus core protein, the basic domain, the linker sequence and the protease domain comprise amino acid residues M(1) to Q(94), P(95) to D(113), and R(114) to W(264), respectively. Core protein domain beginning at M(106) does not bind to the 60S ribosomal subunit, whereas core protein domain beginning at Q(94) binds to the 60S ribosomal subunit and inhibits the disassembly of cores in vitro
695938
Sindbis virus
?
-
-
-
-
additional information
the active site of the protease releases the core protein from the growing polyprotein containing all structural proteins during translation. Core protein is associated to the large 60S ribosomal subunit during in vitro protein synthesis and in the infected cell
695938
Semliki forest virus
?
-
-
-
-
Synonyms
Synonyms
Commentary
Organism
core protein
-
Chikungunya virus
core protein
-
Ross River virus
core protein
-
Semliki forest virus
core protein
-
Sindbis virus
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
additional information
the disassembly of cores is stimulated by increasing the concentration of NaCl, but neither octylglucoside nor low pH stimulates the reaction
Semliki forest virus
additional information
cores, which are resistant to trypsin at physiological salt concentrations, whereas become trypsin sensitive at elevated salt concentrations and under these conditions, the carboxy-terminal domain, beginning with position M(106) is released as a soluble protein. Use of endoproteinase LysC instead of trypsin allows a somewhat larger soluble carboxy-terminal domain beginning with Q(94). The disassembly of cores is stimulated by increasing the concentration of NaCl in the reaction, by the presence of octylglycoside, and by lowering the pH of the reaction to 6.0 and is not stimulated by the presence of NP 40
Sindbis virus
Application (protein specific)
Application
Commentary
Organism
drug development
alphavirus core protein is a target for antiviral chemotherapy
Chikungunya virus
drug development
alphavirus core protein is a target for antiviral chemotherapy
Semliki forest virus
drug development
alphavirus core protein is a target for antiviral chemotherapy
Sindbis virus
Crystallization (Commentary) (protein specific)
Crystallization
Organism
at 25 A resolution
Ross River virus
at 9 A resolution, the C-terminal domain folds into a trypsin-like protease structure
Semliki forest virus
at 9 A resolution, the carboxyterminal domain folds into a trypsin-like protease structure
Sindbis virus
Engineering (protein specific)
Protein Variants
Commentary
Organism
drug development
alphavirus core protein is a target for antiviral chemotherapy
Ross River virus
additional information
mutants containing deletions of residues P(105) to D(118) and M(111) to D(118) in the core protein are viable, but the specific infectivity of these viruses is about 10fold less than the infectivity of wild-type virus. After lysis of infected cells or virus particles, mutant core protein with deletion of residues Q(40) to R(118) behaves as a monomer, whereby the core is generated during virus particle formation by the collection of core protein molecules by the viral membrane proteins prior to and/or during assembly of the viral surface proteins into an icosahedral shell
Semliki forest virus
additional information
mutant containing a deletion of residues K(97) to M(106), wild-type-like cores are assembled in the cytoplasm, and particle formation is largely unaffected, but 26S subgenomic viral RNA, which is not incorporated into wild-type particles, is efficiently packaged into cores and virus particles. Mutations in the linker region and in neighbouring regions of the core protein have no effect on disassembly of viral cores during virus entry
Sindbis virus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
additional information
the carboxy-terminal amino acid residues of the core protein remain associated to the active site after cleavage and thereby inactivate the enzyme
Semliki forest virus
additional information
the carboxy-terminal amino acid residues of the core protein remain associated to the active site after cleavage and thereby inactivate the enzyme
Sindbis virus
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
additional information
in the host, the core protein is transferred to ribosomes, the ribosome bound core protein is distributed throughout the cytoplasm, whereas the genome RNA remains associated with vacuolar membranes
Semliki forest virus
-
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
additional information
the active site of the protease releases the core protein from the growing polyprotein containing all structural proteins during translation. A short linker sequence connects the basic domain to the protease domain. In the Sindbis virus core protein, the basic domain, the linker sequence and the protease domain comprise amino acid residues M(1) to Q(94), P(95) to D(113), and R(114) to W(264), respectively. Core protein domain beginning at M(106) does not bind to the 60S ribosomal subunit, whereas core protein domain beginning at Q(94) binds to the 60S ribosomal subunit and inhibits the disassembly of cores in vitro
695938
Sindbis virus
?
-
-
-
-
additional information
the active site of the protease releases the core protein from the growing polyprotein containing all structural proteins during translation. Core protein is associated to the large 60S ribosomal subunit during in vitro protein synthesis and in the infected cell
695938
Semliki forest virus
?
-
-
-
-
Other publictions for EC 3.4.21.90
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
695938
Wengler
The regulation of disassembly ...
Chikungunya virus, Ross River virus, Semliki forest virus, Sindbis virus
Arch. Virol.
154
381-390
2009
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4
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3
3
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2
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1
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2
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699899
Warrier
Role of sindbis virus capsid p ...
Sindbis virus
J. Virol.
82
4461-4470
2008
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1
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35
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3
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1
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1
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1
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1
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35
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1
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1
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29850
Tong
Refined structure of Sindbis v ...
Sindbis virus
J. Mol. Biol.
230
228-247
1993
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1
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1
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1
1
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2
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2
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1
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1
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1
1
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2
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29851
Kräusslich
Viral proteinases ...
Sindbis virus
Annu. Rev. Biochem.
57
701-754
1988
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1
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1
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