Structure of the human NF-κB p52 homodimer-DNA complex at 2.1 Å resolution
Structure of the human NF-κB p52 homodimer-DNA complex at 2.1 Å resolution
复制标题
DOI：
10.1093/emboj/16.23.7078
复制
发表时间：
1997-12-01
期刊：
影响因子：
11.4
通讯作者：
Müller, CW
中科院分区：
文献类型：
--
作者：
Cramer, P;Larson, CJ;Müller, CW
人 NF-kappa B p52 与天然 kappa B DNA 结合位点 MHC H-2 的特定复合物的晶体结构已在 2.1 埃分辨率下解析，虽然整体结构类似于 NF-kappa B p50-DNA 复合物，但在“插入区域”内观察到明显差异。不同 Rel 蛋白之间该序列片段的长度不同。与 NF-kappa B p50 相比，紧凑的 α 螺旋插入区元件旋转远离 N 端结构域的核心，打开了一个主要的极性裂隙，插入区为其他蛋白质提供了潜在的相互作用表面，结构的高分辨率揭示了许多介导蛋白质-DNA 界面中相互作用的水分子，Rel 蛋白质-DNA 相互作用的额外复杂性来自于扩展的界面水腔，它将二聚体界面边缘的残基连接到中心 DNA 碱基，观察到的水网络可能解释了 NF-kappa B p52 和 NF-kappa B p50 同二聚体之间结合特异性的差异。
The crystal structure of human NF-kappa B p52 in its specific complex with the natural kappa B DNA binding site MHC H-2 has been solved at 2.1 Angstrom resolution, Whereas the overall structure resembles that of the NF-kappa B p50-DNA complex, pronounced differences are observed within the 'insert region'. This sequence segment differs in length between different Rel proteins. Compared with NF-kappa B p50, the compact alpha-helical insert region element is rotated away from the core of the N-terminal domain, opening up a mainly polar cleft, The insert region presents potential interaction surfaces to other proteins, The high resolution of the structure reveals many water molecules which mediate interactions in the protein-DNA interface, Additional complexity in Rel protein-DNA interaction comes from an extended interfacial water cavity that connects residues at the edge of the dimer interface to the central DNA bases, The observed water network might account for differences in binding specificity between NF-kappa B p52 and NF-kappa B p50 homodimers.