Zinc-dependent structure of a single-finger domain of yeast ADR1.
作者： G Parraga , S. Horvath , A Eisen , W. Taylor , L Hood
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摘要: In the proposed "zinc finger" DNA-binding motif, each repeat unit binds a zinc metal ion through invariant Cys and His residues this drives folding of 30-residue into an independent nucleic acid-binding domain. To obtain structural information, we synthesized single double finger peptides from yeast transcription activator ADR1, assessed metal-binding properties these peptides, as well solution structure metal-stabilized domains, with use variety spectroscopic techniques. A can exist sufficient for zinc-dependent DNA binding. An experimentally determined model is that consistent circular dichroism, one- two-dimensional nuclear magnetic resonance, visual spectroscopy single-finger peptide reconstituted in presence zinc.
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