Issue 7, 2014

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

Abstract

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.

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

Supplementary files

Article information

Article type
Communication
Submitted
18 Apr 2014
Accepted
29 Apr 2014
First published
13 May 2014

Mol. BioSyst., 2014,10, 1753-1756

Author version available

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

A. N. Besold, D. L. Amick and S. L. J. Michel, Mol. BioSyst., 2014, 10, 1753 DOI: 10.1039/C4MB00246F

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