A role for hydrogen bonding in DNA recognition by the non-classical CCHHC type zinc finger, NZF-1
Author:
Affiliation:
1. Department of Pharmaceutical Sciences
2. School of Pharmacy
3. University of Maryland
4. Baltimore, USA
Abstract
Neural Zinc Finger Factor-1 contains six Cys2His2Cys domains; the first histidine participates in a functionally important hydrogen bonding interaction.
Publisher
Royal Society of Chemistry (RSC)
Subject
Molecular Biology,Biotechnology
Link
http://pubs.rsc.org/en/content/articlepdf/2014/MB/C4MB00246F
Reference31 articles.
1. Cysteine and histidine shuffling: mixing and matching cysteine and histidine residues in zinc finger proteins to afford different folds and function
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4. Zinc finger proteins: new insights into structural and functional diversity
5. Minimal Functional Sites Allow a Classification of Zinc Sites in Proteins
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