Fig. 7: The model of coupled folding and binding process of pKID and KIX. | Communications Chemistry

Fig. 7: The model of coupled folding and binding process of pKID and KIX.

From: Phosphorylation regulates the binding of intrinsically disordered proteins via a flexible conformation selection mechanism

Fig. 7: The model of coupled folding and binding process of pKID and KIX.

Before the encountering with KIX, the free pKID adopts flexible conformations and quick transiting between the conformations with HRC formed and the conformations without HRC. The pKID dynamically contact with KIX on multiple “hot-pot” binding sites to form the encounter complex, however, the pro-formed HRC structure would promote the correct binding of pKID to the Tyr658 on KIX. The accurate docking further promote the binding of αB region. The binding with KIX also would induce the folding of C-terminal region of αA and the αB region of pKID. After that, the N-terminus of αA would complete the folding. The folded αA of pKID would rotate to the correct positions on KIX.

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