Designer Zinc Finger Proteins: Tools for Creating Artificial DNA-Binding Functional Proteins
- 1 December 2005
- journal article
- review article
- Published by American Chemical Society (ACS) in Accounts of Chemical Research
- Vol. 39 (1) , 45-52
- https://doi.org/10.1021/ar050158u
Abstract
The design of artificial functional DNA-binding proteins has long been a goal for several research laboratories. The zinc finger proteins, which typically contain many fingers linked in tandem fashion, are some of the most studied DNA-binding proteins. The zinc finger protein's tandem arrangement and its the ability to recognize a wide variety of DNA sequences make it an attractive framework to design novel DNA-binding peptides/proteins. Our laboratory has utilized several design strategies to create novel zinc finger peptides by re-engineering the C2H2-type zinc finger motif of transcription factor Sp1. Some of the engineered zinc fingers have shown nuclease and catalytic functional properties. Based on these results, we present the design strategies for the creation of novel zinc fingers.Keywords
This publication has 39 references indexed in Scilit:
- Designing Transcription Factor Architectures for Drug DiscoveryMolecular Pharmacology, 2004
- The Design of Functional DNA-Binding Proteins Based on Zinc Finger DomainsChemical Reviews, 2003
- Drug discovery with engineered zinc-finger proteinsNature Reviews Drug Discovery, 2003
- Three classes of C2H2 zinc finger proteinsCellular and Molecular Life Sciences, 2001
- Expressing the human genomeNature, 2001
- Differing roles for zinc fingers in DNA recognition: Structure of a six-finger transcription factor IIIA complexProceedings of the National Academy of Sciences, 1998
- Zif268 protein–DNA complex refined at 1.6å: a model system for understanding zinc finger–DNA interactionsStructure, 1996
- Zinc Finger Phage: Affinity Selection of Fingers with New DNA-Binding SpecificitiesScience, 1994
- Zinc Finger-DNA Recognition: Crystal Structure of a Zif268-DNA Complex at 2.1 ÅScience, 1991
- Isolation of cDNA encoding transcription factor Sp1 and functional analysis of the DNA binding domainCell, 1987