Structure of a designed dimeric zinc finger protein bound to DNA.

Abstract

Proteins that employ dimerization domains to bind cooperatively to DNA have a number of potential advantages over monomers with regards to gene regulation. Using a combination of structure-based design and phage display, a dimeric Cys(2)His(2) zinc finger protein has been created that binds cooperatively to DNA via an attached leucine zipper dimerization… (More)

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Cite this paper

@article{Wolfe2003StructureOA, title={Structure of a designed dimeric zinc finger protein bound to DNA.}, author={Scot A. Wolfe and Robert A. Grant and Carl O. Pabo}, journal={Biochemistry}, year={2003}, volume={42 46}, pages={13401-9} }