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Publication Abstract from PubMed

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.

Solution structure of a CCHHC domain of neural zinc finger factor-1 and its implications for DNA binding.,Berkovits-Cymet HJ, Amann BT, Berg JM Biochemistry. 2004 Feb 3;43(4):898-903. PMID:14744132^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.