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Dynamic Complexes in CBP

A particularly intriguing example occurs in the complex of the interaction domain of ACTR and the nuclear coactivator binding domain (NCBD) of CBP. CD spectra show that although neither of the free proteins is cooperatively folded, the complex is folded and stable. The 3D structure of the complex [23] demonstrates one of the rationales for the existence of intrinsically unstructured proteins the surface area of contact between the two proteins (Fig. 6.5) is much larger than could be expected from the interaction of folded proteins of comparable size, as has been pointed out [29]. [Pg.126]

Another functional application of intrinsically unstructured proteins is illustrated by the complex between the TAZ1 domain of CBP and the interaction domain of the hypoxia-inducible factor, HIF-la. Like the KIX-pKID complex, the TAZl-HIF-la complex involved the folding of an unstructured [Pg.126]


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