Structure-function relations in transcription factors

Molecular dynamics simulations can provide models of proteins that lack a stable structure.

Protein structure-function relations are central to our understanding of how proteins exert their diverse molecular function with high precision. Most of our knowledge on structure-function relations is based on insight gained into structured proteins. Relatively little is known about proteins that lack a well-defined three-dimensional structure as for example a large number of eukaryotic transcription factors.

Glucosinolate profiles are controlled by six R2R3 domain MYB transcription factors and their interactions with three bHLH transcription factors. Although the expression patterns of the MYB transcription factors strongly overlap, individual MYB transcription factors can be linked to distinct glucosinolate phenotypes. We hypothesize that this is, due to differences in protein structure and/or specific regulatory mechanisms acting at the protein level. By studying the dynamic structure the MYB transcription factors that regulate glucosinolate, we expect to improve the general understanding of structure-function relationships in transcription factor specificity.

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Millard PS, Weber K, Kragelund BB, Burow M (2019) Specificity of MYB interactions relies on motifs in ordered and disordered contexts. Nucleic Acid Research. DOI:10.1093/nar/gkz691.

Millard PS, Kragelund BB, Burow M (2019) R2R3 MYB Transcription Factors – Functions outside the DNA-Binding Domain. Trends in Plant Science. DOI:10.1016/j.tplants.2019.07.003.

Millard PS, Bugge K, Marabini R, Boomsma W, Burow M, Kragelund BB (2019) IDDomainSpotter: Compositional bias reveals domains in long disordered protein regions—Insights from transcription factors. Protein Science. DOI:10.1002/pro.3754