文摘
The design of artificial functional DNA-binding proteins has longbeen a goal for several research laboratories. The zinc fingerproteins, which typically contain many fingers linked in tandemfashion, are some of the most studied DNA-binding proteins. Thezinc finger protein's tandem arrangement and its the ability torecognize a wide variety of DNA sequences make it an attractiveframework to design novel DNA-binding peptides/proteins. Ourlaboratory has utilized several design strategies to create novel zincfinger peptides by re-engineering the C2H2-type zinc finger motifof transcription factor Sp1. Some of the engineered zinc fingershave shown nuclease and catalytic functional properties. Based onthese results, we present the design strategies for the creation ofnovel zinc fingers.