OAS2 dimerizes

Stable Identifier
Reaction [binding]
Homo sapiens
Related Species
Respiratory syncytial virus
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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
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