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 |
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Hauptverfasser: | , , |
Format: | Artikel |
Sprache: | eng |
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Online-Zugang: | Volltext |
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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. |
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ISSN: | 1742-206X 1742-2051 |
DOI: | 10.1039/c4mb00246f |