Solution structure of a CCHHC domain of neural zinc finger factor-1 and its implications for DNA binding

Biochemistry. 2004 Feb 3;43(4):898-903. doi: 10.1021/bi035159d.


The structure of a CCHHC zinc-binding domain from neural zinc finger factor-1 (NZF-1) has been determined in solution though the use of NMR methods. This domain is a member of a family of domains that have the Cys-X(4)-Cys-X(4)-His-X(7)-His-X(5)-Cys consensus sequence. The structure determination reveals a novel fold based around a zinc(II) ion coordinated to three Cys residues and the second of the two conserved His residues. The other His residue is stacked between the metal-coordinated His residue and a relatively conserved aromatic residue. Analysis of His to Gln sequence variants reveals that both His residues are required for the formation of a well-defined structure, but neither is required for high-affinity metal binding at a tetrahedral site. The structure suggests that a two-domain protein fragment and a double-stranded DNA binding site may interact with a common two-fold axis relating the two domains and the two half-sites of the DNA-inverted repeat.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Motifs / genetics
  • Amino Acid Sequence
  • Animals
  • Binding Sites / genetics
  • Cysteine / chemistry
  • DNA / chemistry*
  • DNA / genetics
  • DNA / metabolism*
  • DNA Mutational Analysis
  • Histidine / chemistry
  • Molecular Sequence Data
  • Nerve Tissue Proteins / chemistry*
  • Nerve Tissue Proteins / genetics
  • Nerve Tissue Proteins / metabolism*
  • Nuclear Magnetic Resonance, Biomolecular
  • Peptide Fragments / chemistry
  • Peptide Fragments / genetics
  • Peptide Fragments / metabolism
  • Protein Binding / genetics
  • Protein Structure, Tertiary / genetics
  • Rats
  • Thermodynamics
  • Trans-Activators / chemistry*
  • Trans-Activators / genetics
  • Trans-Activators / metabolism*
  • Zinc / chemistry
  • Zinc Fingers* / genetics


  • Myt1l protein, rat
  • Nerve Tissue Proteins
  • Peptide Fragments
  • Trans-Activators
  • Histidine
  • DNA
  • Zinc
  • Cysteine