A role for hydrogen bonding in DNA recognition by the non-classical CCHHC type zinc finger, NZF-1Electronic supplementary information (ESI) available: Experimental details and characterization data, UV-visible and EPR spectra, table of dissociation constants. See DOI: 10.1039/c4mb00246f

The non-classical zinc finger protein, Neural Zinc Finger Factor-1, contains six Cys 2 His 2 Cys 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. Neural Zinc Finger Factor-1 contains six Cys 2 His 2 Cys domains; the first histidine participates in a functionally important hydrogen bonding interaction.