Homeodomain protein monomer binding

Monomers of homeodomain proteins bind to DNA through a helix-turn-helix motif... 

TFIIA and TFIIB bind to both TBP and DNA Flomeodomain proteins are involved in the development of many eucaryotic organisms Monomers of homeodomain proteins bind to DNA through a heltx-turn-helix motif In vivo specificity of homeodomain... 

The homeodomain frequently binds to DNA as a monomer, in contrast to procaryotic DNA-binding proteins containing tbe belix-turn-helix motif, which usually bind as dimers. In vitro tbe homeodomain binds specifically to... 

How is the binding specificity of the heterodimer achieved compared with the specificity of Mat a2 alone The crystal structure rules out the simple model that the contacts made between the Mat a2 homeodomain and DNA are altered as a result of heterodimerization. The contacts between the Mat o2 homeodomain and DNA in the heterodimer complex are virtually indistinguishable from those seen in the structure of the Mat o2 monomer bound to DNA. However, there are at least two significant factors that may account for the increased specificity of the heterodimer. First, the Mat al homeodomain makes significant contacts with the DNA, and the heterodimeric complex will therefore bind more tightly to sites that provide the contacts required by both partners. Second, site-directed mutagenesis experiments have shown that the protein-protein interactions involving the... 

Whereas amino acid sequence comparisons suggested that the homeodomain would contain a helix-turn-helix motif, the 60-residue homeodomain forms a stable structure that can bind to DNA as a monomer. The recognition helix in the homeodomain is longer and makes more contacts with the DNA core than the recognition helices from bacterial regulatory proteins (fig. 31.18). 

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