A role for hydrogen bonding in DNA recognition by the non-classical CCHHC type zinc finger, NZF-1

The non-classical zinc finger protein, Neural Zinc Finger Factor-1, contains six Cys2His2Cys domains. All three cysteines and the second histidine directly bind Zn(II). Using a combination of mutagenesis, metal coordination and DNA binding studies, we report that the first histidine is involved in a...

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Veröffentlicht in:Molecular bioSystems 2014-01, Vol.10 (7), p.1753-1756
Hauptverfasser: Besold, Angelique N, Amick, Deborah L, Michel, Sarah L J
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Sprache:eng
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Zusammenfassung:The non-classical zinc finger protein, Neural Zinc Finger Factor-1, contains six Cys2His2Cys domains. All three cysteines and the second histidine directly bind Zn(II). Using a combination of mutagenesis, metal coordination and DNA binding studies, we report that the first histidine is involved in a functionally important hydrogen bonding interaction.
ISSN:1742-206X
1742-2051
DOI:10.1039/c4mb00246f