ArticleMolecular biology reports2011
Using the recognition code to swap homeodomain target specificity in cell culture.
Article in Molecular biology reports, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
- Binding polymorphism in the DNA bound state of the Pdx1 homeodomain.PLoS computational biology · 2013Article
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Authors and funding
4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The homeodomain (HD) is a 60 amino acid-long DNA-binding domain. A large fraction of HDs binds with high affinity sequences containing the 5'-TAAT-3' core motif. However, NK-2 class HDs recognizes sequences containing the 5'-CAAG-3' core motif. By using a cell transfection approach, here we show that modification of residues located in the N-terminal arm (at positions 6, 7 and 8) and in the recognition helix (at position 54) is enough to swap the "in vivo" binding specificity of TTF-1 HD (which is a member of the NK-2 class HD) from 5'-CAAG-3' to 5'-TAAT-3'-containing targets. The role of residue at position 54 is also supported by data obtained with the HD of the Drosophila engrailed protein. These data support the notion that DNA-binding specificity "in vivo" is dictated by few critical residues.
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