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Related Experiment Videos

Nucleic acid recognition by OB-fold proteins.

Douglas L Theobald1, Rachel M Mitton-Fry, Deborah S Wuttke

  • 1Department of Chemistry and Biochemistry, University of Colorado at Boulder, Boulder, Colorado 80309-0215, USA. theobal@colorado.edu

Annual Review of Biophysics and Biomolecular Structure
|February 25, 2003
PubMed
Summary

The OB-fold domain is crucial for recognizing nucleic acids. Despite sequence diversity, conserved structural features and binding patterns suggest a common evolutionary origin, not convergent evolution.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • The OB-fold is a common structural motif involved in nucleic acid binding.
  • Understanding the structural basis of OB-fold/nucleic acid interactions is key to deciphering their biological roles.

Purpose of the Study:

  • To analyze structural similarities and differences in OB-fold/nucleic acid complexes.
  • To identify conserved features in OB-fold structure and nucleic acid recognition.

Main Methods:

  • Comparative structural analysis of known OB-fold/nucleic acid complexes.
  • Identification of common structural determinants and binding interactions.

Main Results:

  • OB-fold family members show low sequence similarity but share structural determinants.

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  • Conserved features include binding surface location, nucleic acid polarity, and specific interaction types.
  • Variable loops within the OB-fold core contribute to functional diversity.

    • Conclusions:

    • Conserved nucleic acid binding polarity suggests a monophyletic origin for OB-folds.
    • The OB-fold family likely did not arise through convergent evolution.