Cloned (Comment) | Organism |
---|---|
viperin from monocytic cells, DNA and amino acid sequence determination and analysis, expression of His-tagged full-length enzyme, and of His-tagged viperin (45-361) and viperin (214-361) in Escherichia coli strain BL21 | Homo sapiens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | [4Fe-4S] cluster | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged full-length enzyme and viperin (214-361) from Escherichia coli strain BL21 inclusion bodies, solubilization by 8 M urea and purification by nickel affinity chromatography and gel filtration | Homo sapiens |
Renatured (Comment) | Organism |
---|---|
recombinant soluble His-tagged viperin (45-361) from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, recombinant His-tagged full-length enzyme and viperin (214-361) from Escherichia coli strain BL21 inclusion bodies is solubilized by 8 M urea and further renaturated and purificated by nickel affinity chromatography and gel filtration. Reconstitution of the [4Fe-4S] cluster in Viperin residues 45-361, overview | Homo sapiens |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
monocyte | - |
Homo sapiens | - |
Subunits | Comment | Organism |
---|---|---|
More | structure analysis of recombinant His-tagged viperin (214-361) by UV-visible, circular dichroism, and NMR spectroscopy, overview | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
viperin | - |
Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
S-adenosyl-L-methionine | - |
Homo sapiens | |
[4Fe-4S]-center | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
physiological function | viperin is an interferon-inducible protein inhibiting a diverse spectrum of DNA and RNA viruses. It contains an N-terminal transmembrane helix, a highly conserved C-terminus and a middle region carrying a CX3CX2C motif, characteristic of radical S-adenosyl-L-methionine enzymes. The radical SAM enzyme activity may play a key role in the broad antiviral actions of viperin | Homo sapiens |