Literature summary for 4.6.1.19 extracted from

Han, Y.; Donovan, J.; Rath, S.; Whitney, G.; Chitrakar, A.; Korennykh, A.
Structure of human RNase L reveals the basis for regulated RNA decay in the IFN response (2014), Science, 343, 1244-1248.

Search for more literature for 4.6.1.19

Activating Compound

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 (Commentary)

Crystallization (Comment)	Organism
analysis of two crystal structures of human enzyme	Homo sapiens

Protein Variants

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

Localization	Comment	Organism	GeneOntology No.	Textmining

Natural Substrates/ Products (Substrates)

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

Organism	UniProt	Comment	Textmining
Homo sapiens	Q05823	-	-

Reaction

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	a

Source Tissue

Source Tissue	Comment	Organism	Textmining
HeLa cell	-	Homo sapiens	-

Substrates and Products (Substrate)

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

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

Synonyms	Comment	Organism
RNase L	-	Homo sapiens

General Information

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

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Release 2023.1 (January 2023)