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Fig. 3. Allostery mediated by IDRs. (A) A schematic illustration is shown for positive allosteric coupling between the TAZ2 domain of CBP and the pocket domain of pRB that are bound to the distinct regions (N-terminal region and conserved region 1) of the adenoviral oncoprotein E1A. Truncation of the N-terminal region of E1A drives a transition in allostery from positive to negative coupling. (B) A schematic illustration is shown for the core complex of the NPC in which Nup53 utilizes the N and C-terminal IDRs to recruit Nic96 and Nup157, respectively. Binding of a karyopherin (Kap121) to the C-terminal IDR allosterically destabilizes the core complex by dissociating Nup157 from the nearby binding site and reducing the affinity of Nic96 for Nup53 by about an order of magnitude.
Mol. Cells 2020;43:899~908 https://doi.org/10.14348/molcells.2020.0186
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