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OAS2 dimerizes
Stable Identifier
R-HSA-8985097
Type
Reaction [binding]
Species
Homo sapiens
Related Species
Human respiratory syncytial virus A
Compartment
cytosol
ReviewStatus
5/5
Locations in the PathwayBrowser
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Immune System (Homo sapiens)
Cytokine Signaling in Immune system (Homo sapiens)
Interferon Signaling (Homo sapiens)
Antiviral mechanism by IFN-stimulated genes (Homo sapiens)
OAS antiviral response (Homo sapiens)
OAS2 dimerizes (Homo sapiens)
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Gel filtration experiments using extracts from IFN-treated human HeLa and Daudi cells showed that 2',5'-oligoadenylate (2-5A) synthetase (OAS2, p69) exists as a dimer of 160 kDa (Marie I et al. 1990). Biochemical and mutational studies demonstrated that dimerization of OAS2 protein is required for its enzyme activity (Sarkar SN et al. 1999). Further, photo affinity cross-linking and peptide mapping to study the substrate binding sites in OAS2 have suggested that OAS2 is active only as a dimer because it catalyzes the joining of the acceptor substrate bound to one subunit to the donor substrate bound to the other subunit (Sarkar SN et al. 2002).
Literature References
PubMed ID
Title
Journal
Year
9407111
Enzymatic activity of 2'-5'-oligoadenylate synthetase is impaired by specific mutations that affect oligomerization of the protein
Sarkar, SN
,
Guo, W
,
Sen, GC
,
Ghosh, A
,
Bandyopadhyay, S
J. Biol. Chem.
1997
Participants
Input
x 2
OAS2:OAS2 ligand [cytosol]
(Homo sapiens)
Output
OAS2:OAS2 ligand dimer [cytosol]
(Homo sapiens)
Participates
as an event of
OAS antiviral response (Homo sapiens)
Authored
Shamovsky, V (2017-03-27)
Reviewed
D'Eustachio, P (2017-12-02)
Silverman, RH (2018-07-31)
Created
Shamovsky, V (2017-04-12)
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