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Abstract：
As part of the efforts to understand nuclear IκB function in NF-κB-dependent gene expression, we report an X-ray crystal structure of the IκBζ ankyrin repeat domain in complex with the dimerization domain of the NF-κB p50 homodimer. IκBζ possesses an N-terminal α helix that conveys domain folding stability. Affinity and specificity of the complex depend on a small portion of p50 at the nuclear localization signal. The model suggests that only one p50 subunit supports binding with IκBζ, and biochemical experiments confirm that IκBζ associates with DNA-bound NF-κB p50:RelA heterodimers. Comparisons of IκBζ:p50 and p50:κB DNA complex crystallographic models indicate that structural rearrangement is necessary for ternary complex formation of IκBζ and p50 with DNA.
摘要：
作为了解NF-κB依赖性基因表达中核IκB功能的一部分，我们报道了与NF-κBp50同二聚体的二聚化结构域复合物中IκBζ锚蛋白重复结构域的X射线晶体结构。IκBζ具有N末端α螺旋，可传递结构域折叠稳定性。复合物的亲和力和特异性取决于核定位信号处的p50的一小部分。该模型表明，只有一个p50亚基支持与IκBζ的结合，和生化实验证实，IκBζ与DNA结合的NF-κBp50：RelA异二聚体结合。IκBζ：p50和p50：κBDNA复合物晶体学模型的比较表明，结构重排对于IκBζ和p50与DNA形成三元复合物是必需的。
