Zinc finger proteins: getting a grip on RNA

Curr Opin Struct Biol. 2005 Feb;15(1):94-8. doi: 10.1016/j.sbi.2005.01.006.


C2H2 (Cys-Cys-His-His motif) zinc finger proteins are members of a large superfamily of nucleic-acid-binding proteins in eukaryotes. On the basis of NMR and X-ray structures, we know that DNA sequence recognition involves a short alpha helix bound to the major groove. Exactly how some zinc finger proteins bind to double-stranded RNA has been a complete mystery for over two decades. This has been resolved by the long-awaited crystal structure of part of the TFIIIA-5S RNA complex. A comparison can be made with identical fingers in a TFIIIA-DNA structure. Additionally, the NMR structure of TIS11d bound to an AU-rich element reveals the molecular details of the interaction between CCCH fingers and single-stranded RNA. Together, these results contrast the different ways that zinc finger proteins bind with high specificity to their RNA targets.

Publication types

  • Review

MeSH terms

  • Binding Sites
  • DNA-Binding Proteins / chemistry*
  • Models, Chemical*
  • Models, Molecular*
  • Nucleic Acid Conformation
  • Protein Binding
  • Protein Conformation
  • RNA-Binding Proteins / chemistry*
  • Structure-Activity Relationship
  • Zinc Fingers*


  • DNA-Binding Proteins
  • RNA-Binding Proteins