Literature summary extracted from
Huang, H.; Zeqiraj, E.; Dong, B.; Jha, B.K.; Duffy, N.M.; Orlicky, S.; Thevakumaran, N.; Talukdar, M.; Pillon, M.C.; Ceccarelli, D.F.; Wan, L.C.; Juang, Y.C.; Mao, D.Y.; Gaughan, C.; Brinton, M.A.; Perelygin, A.A.; Kourinov, I.; Guarne, A.; Silverman, R.H.; Sicheri, F.
Dimeric structure of pseudokinase RNase L bound to 2-5A reveals a basis for interferon-induced antiviral activity (2014), Mol. Cell, 53, 221-234.
Activating Compound
EC Number |
Activating Compound |
Comment |
Organism |
Structure |
---|
4.6.1.19 |
2',5'-Oligoadenylate |
the enzyme's pseudokinase domain is involved in the natural activator sensing, binding site and structure, modeling, overview. Quantitative determination of specific binding of the full-length enzyme and of isolated enzyme ANK domain to immobilized biotinylated 2',5'-oligoadenylate |
Homo sapiens |
|
4.6.1.19 |
2',5'-Oligoadenylate |
the enzyme's pseudokinase domain is involved in the natural activator sensing, binding site and structure, modeling, overview. Quantitative determination of specific binding of the full-length enzyme and of isolated enzyme ANK domain to immobilized biotinylated 2',5'-oligoadenylate |
Sus scrofa |
|
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
4.6.1.19 |
expression of wild-type and mutant enzymes in HeLa-M cell and in Escherichia coli as TEV-cleavable GST fusion proteins |
Sus scrofa |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
4.6.1.19 |
enzyme with bound natural activator 2',5'-oligoadenylate and with and without ADP or the nonhydrolysable ATP mimetic AMP-PNP, X-ray diffraction structure determination and analysis at 2.5 A resolution and small-angle X-ray scattering structure determination and analysis at 3.25 A resolution |
Sus scrofa |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
4.6.1.19 |
K390R |
the mutation in the kinase ATP binding site of the nezyme results in greatly impaired RNase activity |
Sus scrofa |
4.6.1.19 |
K392R |
the mutation in the kinase ATP binding site of the nezyme results in greatly impaired RNase activity |
Homo sapiens |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
4.6.1.19 |
Homo sapiens |
- |
- |
- |
4.6.1.19 |
Sus scrofa |
- |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
4.6.1.19 |
recombinant GST-tagged wild-type and mutant enzymes from Escherichia coli by glutathione affinity chromatography and TEV-cleavage |
Sus scrofa |
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
4.6.1.19 |
dimer |
the dimer configuration of full-length enzyme arises from the intertwining of two promoters through a 155° twisting action across the ANK domain-PK domain junction, which gives rise to the appearance of an exchange of ANK and PK domains between protomers, back-to-back dimer arrangement. Dimerization of the ANK domain is facilitated by a head-to-tail arrangement with concave surfaces facing inward. Kinase domain-ANK domain contacts, overview |
Homo sapiens |
4.6.1.19 |
dimer |
the dimer configuration of full-length enzyme arises from the intertwining of two promoters through a 155° twisting action across the ANK domain-PK domain junction, which gives rise to the appearance of an exchange of ANK and PK domains between protomers, back-to-back dimer arrangement. Dimerization of the ANK domain is facilitated by a head-to-tail arrangement with concave surfaces facing inward. Kinase domain-ANK domain contacts, overview |
Sus scrofa |
4.6.1.19 |
More |
consisting of nine alpha helices with a 19-residue disordered sequence (residues 644-662, harboring a 12-residue porcine-specific insertion) between helices alpha3 and alpha4, RNase domain structure, overview. The ANK domain of porcine RNase L adopts a crescent-shaped structure consisting of a stack of nine ankyrin repeats, each possessing a characteristic loop-helix1-loop-helix2-loop architecture |
Sus scrofa |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
4.6.1.19 |
RNase L |
- |
Homo sapiens |
4.6.1.19 |
RNase L |
- |
Sus scrofa |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
4.6.1.19 |
evolution |
involvement of the pseudokinase domain of the enzyme cofactor sensing, nucleotide binding, dimerization, and ribonuclease functions highlights the evolutionary adaptability of the eukaryotic protein kinase fold |
Homo sapiens |
4.6.1.19 |
evolution |
involvement of the pseudokinase domain of the enzyme cofactor sensing, nucleotide binding, dimerization, and ribonuclease functions highlights the evolutionary adaptability of the eukaryotic protein kinase fold |
Sus scrofa |
4.6.1.19 |
additional information |
involvement of the pseudokinase domain of the enzyme activator sensing, nucleotide binding, dimerization, and ribonuclease functions |
Homo sapiens |
4.6.1.19 |
additional information |
involvement of the pseudokinase domain of the enzyme activator sensing, nucleotide binding, dimerization, and ribonuclease functions |
Sus scrofa |
4.6.1.19 |
physiological function |
RNase L is an ankyrin repeat domain-containing dual endoribonuclease-pseudokinase that is activated by unusual 2',5'-oligoadenylate second messengers and impedes viral infections in higher vertebrates. The enzyme is important in interferon-regulated antiviral innate immunity. Molecular basis for the regulation of the enzyme's antiviral function, overview |
Homo sapiens |
4.6.1.19 |
physiological function |
RNase L is an ankyrin repeat domain-containing dual endoribonuclease-pseudokinase that is activated by unusual 2',5'-oligoadenylate second messengers and impedes viral infections in higher vertebrates. The enzyme is important in interferon-regulated antiviral innate immunity. Molecular basis for the regulation of the enzyme's antiviral function, overview |
Sus scrofa |