| Автор | Theobald, Douglas L. |
| Автор | Mitton-Fry, Rachel M. |
| Автор | Wuttke, Deborah S. |
| Дата выпуска | 2003 |
| dc.description | ▪ Abstract The OB-fold domain is a compact structural motif frequently used for nucleic acid recognition. Structural comparison of all OB-fold/nucleic acid complexes solved to date confirms the low degree of sequence similarity among members of this family while highlighting several structural sequence determinants common to most of these OB-folds. Loops connecting the secondary structural elements in the OB-fold core are extremely variable in length and in functional detail. However, certain features of ligand binding are conserved among OB-fold complexes, including the location of the binding surface, the polarity of the nucleic acid with respect to the OB-fold, and particular nucleic acid–protein interactions commonly used for recognition of single-stranded and unusually structured nucleic acids. Intriguingly, the observation of shared nucleic acid polarity may shed light on the longstanding question concerning OB-fold origins, indicating that it is unlikely that members of this family arose via convergent evolution. |
| Формат | application.pdf |
| Издатель | Annual Reviews |
| Копирайт | Annual Reviews |
| Название | NUCLEIC ACID RECOGNITION BY OB-FOLD PROTEINS |
| DOI | 10.1146/annurev.biophys.32.110601.142506 |
| Print ISSN | 1056-8700 |
| Журнал | Annual Review of Biophysics and Biomolecular Structure |
| Том | 32 |
| Первая страница | 115 |
| Последняя страница | 133 |
| Аффилиация | Theobald, Douglas L.; Department of Chemistry and Biochemistry, University of Colorado at Boulder, Boulder, Colorado 80309-0215; email: theobal@colorado.edu fryrm@colorado.edu deborah.wuttke@colorado.edu |
