Ghosh G, van Duyne G, Ghosh S, Sigler P B
Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06510.
Nature. 1995 Jan 26;373(6512):303-10. doi: 10.1038/373303a0.
The 2.3-A crystal structure of the transcription factor NK-kappa B p50 homodimer bound to a palindromic kappa B site reveals that the Rel homology region folds into two distinct domains, similar to those in the immunoglobulin superfamily. The p50 dimer envelopes an undistorted B-DNA helix, making specific contacts along the 10-base-pair kappa B recognition site mainly through loops connecting secondary structure elements in both domains. The carboxy-terminal domains form a dimerization interface between beta-sheets using residues that are strongly conserved in the Rel family.
与回文κB位点结合的转录因子NK-κB p50同二聚体的2.3埃晶体结构表明，Rel同源区域折叠成两个不同的结构域，类似于免疫球蛋白超家族中的结构域。p50二聚体包裹着一个未扭曲的B-DNA螺旋，主要通过连接两个结构域中二级结构元件的环沿着10个碱基对的κB识别位点进行特异性接触。羧基末端结构域利用Rel家族中高度保守的残基在β-折叠之间形成二聚化界面。
