EC Number   |
Subunits |
Reference |
|---|
   2.7.7.84 | ? |
x * 34700, calculated |
737791 |
| 2.7.7.84 | ? |
x * 35748, seuence calculation, x * 35000, SDS-PAGE |
723200 |
| 2.7.7.84 | ? |
x * 39200, recombinant FLAG-tagged OAS2 domain I, SDS-PAGE, x * 41500, FLAG-tagged OAS2 domain II, x * 69000, recombinant full-length FLAG-tagged OAS2, SDS-PAGE |
760514 |
| 2.7.7.84 | ? |
x * 42000, OAS1, SDS-PAGE |
722991 |
| 2.7.7.84 | ? |
x * 43000, about, OAS1A, sequence calculation |
723243 |
| 2.7.7.84 | dimer |
2 * 56000-59000, isozyme OAS2, two dimers form a tetramer, SDS-PAGE |
721753 |
| 2.7.7.84 | homotetramer |
4 * 56000-59000, isozyme OAS1, SDS-PAGE |
721753 |
| 2.7.7.84 | More |
three distinct forms of 2'-5'OAS exist in human cells, small, medium, and large, which contain one, two, and three OAS units, respectively, and are encoded by distinct genes clustered on the 2'-5OAS locus on human chromosome 12. The monomeric OAS-like protein, OASL, is catalytically inactive |
721753 |
| 2.7.7.84 | 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 |
722991 |
| 2.7.7.84 | More |
zinc ions can control the oligomerisation by enhancing the formation of tetrameric forms of OAS1p42 |
722256 |
