Sandbox Reserved 1485: Difference between revisions
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== | == Importance of the tandem PHD-Bromodomain == | ||
Kap-1 structure have a tandem PHD finger- bromodomain. This tandem is implicate in the repression of specific gene. The tandem is formed with the first helix, of an atypical bromodomain which forms a central hydrophobic core. Hence, three helix of the bromodomain and the zinc binding PHD finger are anchored in the central core. The bromodomain adopt four helix bundle ( 100 amino-acid) and the PHD finger contain an antiparallel sheet Béta (60 amino-acid) . Sumoylated Kap-1 is the highly repressive form. That’s why the adjacent KAP-1 bromodomain is sumoylated by the PHD which functioning as an intramolecular E3 ligase. The bromodomain need to be sumoylate because it allows interaction with SETDB1 (SET domain, bifurcated 1) in order to stimule it H3K9me3 specific histone methyltransferase activity. The bromodomain can also interact with Mi2 which is an isoform of the Mi2 protein found in NuRD complex. | |||
== Relevance == | == Relevance == | ||
