| Autor: |
Lewis, Hal A, Musunuru, Kiran, Jensen, Kirk B, Edo, Carme, Chen, Hua, Darnell, Robert B, Burley, Stephen K |
| Jazyk: |
angličtina |
| Zdroj: |
Cell. (3):323-332 |
| ISSN: |
0092-8674 |
| DOI: |
10.1016/S0092-8674(00)80668-6 |
| Popis: |
The structure of a Nova protein K homology (KH) domain recognizing single-stranded RNA has been determined at 2.4 Å resolution. Mammalian Nova antigens (1 and 2) constitute an important family of regulators of RNA metabolism in neurons, first identified using sera from cancer patients with the autoimmune disorder paraneoplastic opsoclonus-myoclonus ataxia (POMA). The structure of the third KH domain (KH3) of Nova-2 bound to a stem loop RNA resembles a molecular vise, with 5′-Ura-Cyt-Ade-Cyt-3′ pinioned between an invariant Gly-X-X-Gly motif and the variable loop. Tetranucleotide recognition is supported by an aliphatic α helix/β sheet RNA-binding platform, which mimics 5′-Ura-Gua-3′ by making Watson-Crick-like hydrogen bonds with 5′-Cyt-Ade-3′. Sequence conservation suggests that fragile X mental retardation results from perturbation of RNA binding by the FMR1 protein. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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