ETV4 and AP1 transcription factors form multivalent interactions with three sites on the MED25 activator-interacting domain

The recruitment of transcriptional cofactors by sequence-specific transcription factors challenges the basis of high affinity and selective interactions. Extending previous studies that the N-terminal activation domain (AD) of ETV5 interacts with Mediator subunit 25 (MED25), we establish that simila...

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Pubblicato in:J Mol Biol
Autori principali: Currie, Simon L., Doane, Jedediah J., Evans, Kathryn S., Bhachech, Niraja, Madison, Bethany J., Lau, Desmond K. W., McIntosh, Lawrence P., Skalicky, Jack J., Clark, Kathleen A., Graves, Barbara J.
Natura: Artigo
Lingua:Inglês
Pubblicazione: 2017
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Article
Accesso online:https://ncbi.nlm.nih.gov/pmc/articles/PMC5632138/
https://ncbi.nlm.nih.gov/pubmed/28728983
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.jmb.2017.06.024
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