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. This journal is
Original language | English (US) |
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Pages (from-to) | 1753-1756 |
Number of pages | 4 |
Journal | Molecular BioSystems |
Volume | 10 |
Issue number | 7 |
DOIs | |
State | Published - Jul 2014 |
Externally published | Yes |
ASJC Scopus subject areas
- Biotechnology
- Molecular Biology