Date: 04 Jan 2018
Multi-modal interactions are frequently observed in intrinsically disordered regions (IDRs) of proteins upon binding to their partners. In many cases, post-translational modifications in IDRs are accompanied by coupled folding and binding. From both molecular simulations and biochemical experiments with mutational studies, we show that the IDR including a Ser rich region (SRR) of the transcription factor Ets1, just before the DNA-binding core domain, undergoes multi-modal interactions when the SRR is not phosphorylated. In the phosphorylated state, the SRR forms a few specific complex structures with the Ets1 core, covering the recognition helix in the core and drastically reducing the DNA binding affinities as the auto-inhibitory state. The binding kinetics of mutated Ets1 indicates that aromatic residues in the SRR can be substituted with other hydrophobic residues for the interactions with the Ets1 core.
For inquiries regarding this press release
E-mail: firstname.lastname@example.org Phone: +81 45 787 2590
E-mail: email@example.com Phone: +81 45 787 2590
Department of Biochemistry,
Yokohama City University Graduate School of Medicine
Fukuura 3-9, Kanazawa-ku, Yokohama, 236-0004 JAPAN