| First Author | Kristiansen H | Year | 2011 |
| Journal | J Interferon Cytokine Res | Volume | 31 |
| Issue | 1 | Pages | 41-7 |
| PubMed ID | 21142819 | Mgi Jnum | J:192649 |
| Mgi Id | MGI:5465529 | Doi | 10.1089/jir.2010.0107 |
| Citation | Kristiansen H, et al. (2011) The oligoadenylate synthetase family: an ancient protein family with multiple antiviral activities. J Interferon Cytokine Res 31(1):41-7 |
| abstractText | The 2'-5' oligoadenylate synthetases (OAS) are interferon-induced antiviral enzymes that recognize virally produced dsRNA and initiate RNA destabilization through activation of RNase L within infected cells. However, recent evidence points toward several RNase L-independent pathways, through which members of the OAS family can exert antiviral activity. The crystal structure of OAS led to a novel insight into the catalytic mechanism, and revealed a remarkable similarity between OAS, Polyadenosine polymerase, and the class I CCA-adding enzyme from Archeoglobus fulgidus. This, combined with a variety of bioinformatic data, leads to the definition of a superfamily of template independent polymerases and proved that the OAS family are ancient proteins, which probably arose as early as the beginning of metazoan evolution. |
