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Showing 1–4 of 4 results
Advanced filters: Author: Andreas Prestel Clear advanced filters

  • The function of transcription factors is conveyed through intrinsically disordered regions (IDRs) containing activation or repression domains, but the lack of quantitative structural ensemble models prevents their mechanistic decoding. Here, the authors use several methods to demonstrate that DNA binding can lead to complex changes in the IDR ensemble and accessibility on the example of the C-terminal IDR of pioneer factor Sox2.

    • Sveinn Bjarnason
    • Jordan A. P. McIvor
    • Pétur O. Heidarsson
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-16

  • Transcription factor DREB2A interacts with Med25 to regulate stress responses. Here, the authors show that DREB2A uses splicing and proline-isomerization for this regulation and that proline cis-trans switching introduces structural frustration facilitating regulator exchange.

    • Frederik Friis Theisen
    • Andreas Prestel
    • Karen Skriver
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-13

  • Hendus-Altenburger et al. provide biochemical, structural and functional information on the lipid interaction domain (LID) of the Na+/H+ Exchanger 1 (NHE1). They find that NHE1-LID is intrinsically disordered, but, when allowed to interact with a lipid membrane, forms a helical αα-hairpin, stabilized by hydrophobic and electrostatic interactions. This co-structure is fundamental for NHE1 activity, giving insight into membrane protein regulation via disordered domains.

    • Ruth Hendus-Altenburger
    • Jens Vogensen
    • Birthe B. Kragelund
    ResearchOpen Access
    Communications Biology
    Volume: 3, P: 1-18