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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2004-1-27
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0006-2960
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
43
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
898-903
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:14744132-Amino Acid Motifs,
pubmed-meshheading:14744132-Amino Acid Sequence,
pubmed-meshheading:14744132-Animals,
pubmed-meshheading:14744132-Binding Sites,
pubmed-meshheading:14744132-Cysteine,
pubmed-meshheading:14744132-DNA,
pubmed-meshheading:14744132-DNA Mutational Analysis,
pubmed-meshheading:14744132-Histidine,
pubmed-meshheading:14744132-Molecular Sequence Data,
pubmed-meshheading:14744132-Nerve Tissue Proteins,
pubmed-meshheading:14744132-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:14744132-Peptide Fragments,
pubmed-meshheading:14744132-Protein Binding,
pubmed-meshheading:14744132-Protein Structure, Tertiary,
pubmed-meshheading:14744132-Rats,
pubmed-meshheading:14744132-Thermodynamics,
pubmed-meshheading:14744132-Trans-Activators,
pubmed-meshheading:14744132-Zinc,
pubmed-meshheading:14744132-Zinc Fingers
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pubmed:year |
2004
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pubmed:articleTitle |
Solution structure of a CCHHC domain of neural zinc finger factor-1 and its implications for DNA binding.
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pubmed:affiliation |
Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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