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- W2022704908 abstract "Computer modeling suggested that transcription factors with novel sequence specificities could be designed by combining known DNA binding domains. This structure-based strategy was tested by construction of a fusion protein, ZFHD1, that contained zinc fingers 1 and 2 from Zif268, a short polypeptide linker, and the homeodomain from Oct-1. The fusion protein bound optimally to a sequence containing adjacent homeodomain (TAATTA) and zinc finger (NGGGNG) subsites. When fused to an activation domain, ZFHD1 regulated promoter activity in vivo in a sequence-specific manner. Analysis of known protein-DNA complexes suggests that many other DNA binding proteins could be designed in a similar fashion." @default.
- W2022704908 created "2016-06-24" @default.
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- W2022704908 date "1995-01-06" @default.
- W2022704908 modified "2023-10-16" @default.
- W2022704908 title "Structure-Based Design of Transcription Factors" @default.
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- W2022704908 doi "https://doi.org/10.1126/science.7809612" @default.
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