Nucleic Acid Recognition by OB-Fold Proteins
- 1 June 2003
- journal article
- review article
- Published by Annual Reviews in Annual Review of Biophysics and Biophysical Chemistry
- Vol. 32 (1), 115-133
- https://doi.org/10.1146/annurev.biophys.32.110601.142506
Abstract
▪ 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.Keywords
This publication has 81 references indexed in Scilit:
- Crystal structure of the 30 s ribosomal subunit from Thermus thermophilus: structure of the proteins and their interactions with 16 s RNAJournal of Molecular Biology, 2002
- Crystal structure of the N-terminal domain of Oxytricha nova telomere end-binding protein α subunit both uncomplexed and complexed with telomeric ssDNAJournal of Molecular Biology, 2001
- DNA G-quartets in a 1.86 Å resolution structure of an Oxytricha nova telomeric protein-DNA complexJournal of Molecular Biology, 2001
- The Complete Atomic Structure of the Large Ribosomal Subunit at 2.4 Å ResolutionScience, 2000
- Validation of protein models from Cα coordinates aloneJournal of Molecular Biology, 1997
- Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNANature, 1997
- MOLMOL: A program for display and analysis of macromolecular structuresJournal of Molecular Graphics, 1996
- Solution Structure of the Anticodon-binding Domain of Escherichia coli Lysyl-tRNA Synthetase and Studies of its Interaction with tRNALysJournal of Molecular Biology, 1995
- Attachment sites of primary binding proteins L1, L2 and L23 on 23 S ribosomal RNA of Escherichia coliJournal of Molecular Biology, 1991
- Telomeric DNA-protein interactions of Oxytricha macronuclear DNA.Genes & Development, 1987