Activating Compound | Comment | Organism | Structure |
---|---|---|---|
2',5'-linked oligoadenylates | two different binding sites in the enzyme's ANK domain and a third site in the N lobe of the KH domain, sensing mechanism, structure-function analysis, overview. The KH/KH and kinase extension nuclease (KEN)/KEN interfaces are important in 2',5'-oligoadenylate-dependent enzyme activation | Homo sapiens |
Crystallization (Comment) | Organism |
---|---|
analysis of two crystal structures of human enzyme | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
H672N | catalytically inactive enzyme mutant | Homo sapiens |
H672N | RNA cleavage enzyme mutant, which shows reduced activity compared to the wild-type enzyme. The H672N mutation eliminates the proton transfer but preserves the H-bonding and space-filling character of histidine. Thus, the H672N mutant interacts with RNA analogous to the wild-type protein but without cleaving the RNA. A single H672N mutant is a potent in trans activator for wild-type RNase L, whereas a double H672N mutant is inactive | Homo sapiens |
additional information | construction of enzyme comprising residues 21-719 | Homo sapiens |
R163A | action potential aI clamp enzyme mutant, which shows reduced activity compared to the wild-type enzyme | Homo sapiens |
R412A | KH/KH interface enzyme mutant, which shows reduced activity compared to the wild-type enzyme | Homo sapiens |
R427A | activator recognition enzyme mutant, which shows reduced activity compared to the wild-type enzyme | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
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Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Homo sapiens | cleavage of biological targets by the enzyme with site selection in mammalian ribosomes and hepatitis C virus RNA, overview | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q05823 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
RNA + H2O = an [RNA fragment]-3'-nucleoside-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment] | mechanism of RNA recognition, binding and cleavage by RNase L, overview | Homo sapiens |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
HeLa cell | - |
Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | cleavage of biological targets by the enzyme with site selection in mammalian ribosomes and hepatitis C virus RNA, overview | Homo sapiens | ? | - |
? | |
additional information | the enzyme cleaves 3' of UN sequences, RNA sequence recognition involves the KEN domain homodimer, RNA cleavage is carried out by the symmetry-related histidine H672 provided by homodimerization, a single H672 residue per a KEN/KEN dimer is necessary and sufficient for RNA cleavage, overview. With Angptl3 mRNA as substrate, RIDD cleavage sites and the consensus UN-N are utilized by RNase L, Cyp1 mRNAs and pre-mir-17microRNA are all cleaved at UG-C sites | Homo sapiens | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | the enzyme forms a crossed homodimer stabilized by ankyrin (ANK) and kinase homology (KH) domains, which positions two kinase extension nuclease (KEN) domains for asymmetric RNA recognition | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
RNase L | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
additional information | structure-function analysis, overview. The KH/KH and kinase extension nuclease (KEN)/KEN interfaces are important in 2',5'-oligoadenylate-dependent enzyme activation | Homo sapiens |