Article
CCHX zinc finger derivatives retain the ability to bind Zn(II) and mediate protein-DNA interactions.
The Journal of biological chemistry - 25 Jul 2003
Simpson Raina J Y, Cram Edward D, Czolij Robert, Matthews Jacqueline M, Crossley Merlin, Mackay Joel P
Abstract excerpt
Classical (CCHH) zinc fingers are among the most common protein domains found in eukaryotes. They function as molecular recognition elements that mediate specific contact with DNA, RNA, or other proteins and are composed of a betabetaalpha fold surrounding a single zinc ion that is ligated by two cysteine and two histidine residues. In a number of variant zinc fingers, the final histidine is not conserved, and in...
Topics
- Amino Acid Sequence
- Animals
- Aspartic Acid
- Circular Dichroism
- Cysteine
- DNA
- DNA-Binding Proteins
- Dose-Response Relationship, Drug
- Histidine
- Humans
- Kinetics
- Magnetic Resonance Spectroscopy
- Models, Molecular