Nucleic Acid Recognition by OB-fold Proteins

Overview

Journal Annu Rev Biophys Biomol Struct

Publisher Annual Reviews

Specialties Biophysics
Molecular Biology

Date 2003 Feb 25

PMID 12598368

Citations 260

Authors

Douglas L Theobald

Rachel M Mitton-Fry

Deborah S Wuttke

Affiliations

Soon will be listed here.

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.

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