| 词条 | 2'-5'-oligoadenylate synthase |
| 释义 |
| Symbol = OAS1_C | Name = 2'-5'-oligoadenylate synthetase 1, domain 2, C-terminus | image = | width = | caption = | Pfam = PF10421 | Pfam_clan = | InterPro = IPR018952 | SMART = | PROSITE = | MEROPS = | SCOP = | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = }} In molecular biology, 2'-5'-oligoadenylate synthetase is an enzyme. It is an antiviral enzyme that counteracts viral attack by degrading viral and host RNA. The enzyme uses ATP in 2'-specific nucleotidyl transfer reactions to synthesize 2'-5'-oligoadenylates, which activate latent ribonuclease (RNASEL), resulting in degradation of viral RNA and inhibition of virus replication.[1] The C-terminal half of 2'-5'-oligoadenylate synthetase, also referred to as domain 2 of the enzyme, is largely alpha-helical and homologous to a tandem ubiquitin repeat. It carries the region of enzymatic activity between (between what?) at the extreme C-terminal end.[2] Human proteins
See also
References1. ^{{cite journal |vauthors=Ghosh SK, Kusari J, Bandyopadhyay SK, Samanta H, Kumar R, Sen GC | title = Cloning, sequencing, and expression of two murine 2'-5'-oligoadenylate synthetases. Structure-function relationships | journal = J. Biol. Chem. | volume = 266 | issue = 23 | pages = 15293–9 |date=August 1991 | pmid = 1651324 | doi = | url = }} {{InterPro content|IPR018952}}2. ^{{cite journal |vauthors=Hartmann R, Justesen J, Sarkar SN, Sen GC, Yee VC | title = Crystal structure of the 2'-specific and double-stranded RNA-activated interferon-induced antiviral protein 2'-5'-oligoadenylate synthetase | journal = Mol. Cell | volume = 12 | issue = 5 | pages = 1173–85 |date=November 2003 | pmid = 14636576 | doi = 10.1016/S1097-2765(03)00433-7| url = }} 1 : Protein domains |
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