Literature summary for 2.7.7.84 extracted from

Meng, H.; Deo, S.; Xiong, S.; Dzananovic, E.; Donald, L.; Van Dijk, C.; McKenna, S.
Regulation of the interferon-inducible 2'-5'-oligoadenylate synthetases by adenovirus VAI RNA (2012), J. Mol. Biol., 422, 635-649.

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Activating Compound

Activating Compound	Comment	Organism	Structure
viral RNA VAI	sequences and secondary structures of adenovirus VAI dsRNAs, overview. Highly structured RNA, VAI, positively regulates the activity of the interferon-induced 2'5'-oligoadenylate synthase, which typically represents a key mechanism whereby host-cell protein translation is attenuated in response to foreign dsRNA. In the contrary, with other cell proteins, RNA VAI, after processing by the RNA silencing machinery, inhibits the innate immune response via a series of interactions with specific protein partners. OAS1:VAI complex stoichiometry and kinetics, overview. The RNA 5'-end phosphorylation state is important in the activation or inhibition of OAS enzymes. While full-length VAI does indeed activate OAS1 in vitro, the Dicer-truncated molecule lacking the terminal stem has the opposite effect, and this is the physiologically important response, overview	Homo sapiens

Cloned(Commentary)

Cloned (Comment)	Organism
expression of tagged isozyme OAS1 in Escherichia coli	Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
42000	-	x * 42000, OAS1, SDS-PAGE	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant tagged isozyme OAS1 from Escherichia coli, cleavage of the tag	Homo sapiens

Subunits

Subunits	Comment	Organism
?	x * 42000, OAS1, SDS-PAGE	Homo sapiens
More	three isozymes of different sizes, the core OAS unit adopts a bilobal conformation in which the catalytic core is located at the junction between the N- and C-terminal domains	Homo sapiens

Synonyms

Synonyms	Comment	Organism
2'-5'-oligoadenylate synthetase	-	Homo sapiens
OAS	-	Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Homo sapiens

Expression

Organism	Comment	Expression
Homo sapiens	induction by interferon	up

General Information

General Information	Comment	Organism
additional information	three major forms of OAS proteins in human cells: 40/46-kDa small isoforms, OAS1, 69/71-kDa medium isoforms, OAS2, and a 100-kDa large isoform, OAS3	Homo sapiens
physiological function	highly structured RNA, VAI, is able to positively regulate the activity of the interferon-induced 2'5'-oligoadenylate synthase, a processed version of VAI lacking the terminal stem behaves as a pseudo-inhibitor of OAS1. The RNA 5'-end phosphorylation state is important in the activation or inhibition of OAS enzymes. While full-length VAI activates OAS1 in vitro, the Dicer-truncated molecule lacking the terminal stem has the opposite effect, and this is the physiologically important response	Homo sapiens

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Release 2023.1 (January 2023)