Article
Structure of a histidine-X4-histidine zinc finger domain: insights into ADR1-UAS1 protein-DNA recognition.
Biochemistry - 19 Apr 1994
Bernstein B E, Hoffman R C, Horvath S, Herriott J R, Klevit R E
Abstract excerpt
The solution structure for a mutant zinc finger peptide based on the sequence of the C-terminal ADR1 finger has been determined by two-dimensional NMR spectroscopy. The mutant peptide, called PAPA, has both proline residues from the wild-type sequence replaced with alanines. A nonessential cystei...
Topics
- Alanine
- Amino Acid Sequence
- Binding Sites
- Cysteine
- DNA
- DNA-Binding Proteins
- Histidine
- Magnetic Resonance Spectroscopy
- Models, Molecular
- Molecular Sequence Data
- Molecular Structure
- Mutation
- Protein Conformation
- Saccharomyces cerevisiae Proteins
- Solutions
- Transcription Factors
- Zinc Fingers