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Annual Review of Biophysics

Volume 32, 2003

Nucleic Acid Recognition by OB-Fold Proteins

Abstract

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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.

Keyword(s): protein fold, single stranded, structural alignment
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2003-06-01
2024-04-25
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Nucleic Acid Recognition by OB-Fold Proteins
Annual Review of Biophysics 32, 115 (2003); https://doi.org/10.1146/annurev.biophys.32.110601.142506
/content/journals/10.1146/annurev.biophys.32.110601.142506
/content/journals/10.1146/annurev.biophys.32.110601.142506
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