Abstract:
: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.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Kasahara K,Shiina M,Higo J,Ogata K,Nakamura Hdoi
10.1093/nar/gkx1297subject
Has Abstractpub_date
2018-03-16 00:00:00pages
2243-2251issue
5eissn
0305-1048issn
1362-4962pii
4788344journal_volume
46pub_type
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