| First Author | Hofsteenge J | Year | 1998 |
| Journal | Cell Mol Life Sci | Volume | 54 |
| Issue | 8 | Pages | 804-10 |
| PubMed ID | 9760989 | Mgi Jnum | J:49885 |
| Mgi Id | MGI:1289359 | Doi | 10.1007/s000180050209 |
| Citation | Hofsteenge J, et al. (1998) Ribonuclease 4, an evolutionarily highly conserved member of the superfamily. Cell Mol Life Sci 54(8):804-10 |
| abstractText | The structural and enzymatic properties of RNase 4 are reviewed. This RNase shows a much higher interspecies similarity (approximately 90%) than the other members of the RNase A superfamily. The enzyme is ubiquitous, with the highest amounts present in liver and lung. Its unique uridine specificity results from alterations in and around the pyrimidine-binding site. In particular, the shortened C-terminus and the side chains of Phe-42, Asp-80 and Arg-101 appear to be involved. RNase 4 binds tightly to the intracellular RNase inhibitor, with a Kd of 4 x 10(-15) M. |
