Uegaki K, Shirakawa M, Harada H, Taniguchi T, Kyogoku Y
Institute for Protein Research, Osaka University, Japan.
FEBS Lett. 1995 Feb 13;359(2-3):184-8. doi: 10.1016/0014-5793(95)00040-g.
The secondary structure elements of the DNA-binding domain of mouse interferon regulatory factor 2 [IRF-2(113)] were determined by heteronuclear multidimensional NMR spectroscopy. The sequential NOE connectivities, amide proton exchange rates, and 3JHN alpha coupling constants indicated the presence of three alpha-helical regions and four short beta-strands connected through relatively long loops. The long range NOEs indicated the four strands form an antiparallel beta-sheet and the three alpha-helices form a bundle on the sheet. The arrangement of the secondary structure elements and the overall folding topology resemble those of the DNA binding domains of bacterial activator CAP, heat shock transcription factors, and fork-head proteins, although there is no sequence homology among them.
通过异核多维核磁共振光谱法确定了小鼠干扰素调节因子2 [IRF-2(113)] 的DNA结合结构域的二级结构元件。序列NOE连接性、酰胺质子交换率和3JHNα耦合常数表明存在三个α-螺旋区域和四个通过相对较长的环连接的短β-链。长程NOE表明四条链形成一个反平行β-折叠片，三个α-螺旋在该片上形成一个束。二级结构元件的排列和整体折叠拓扑结构与细菌激活剂CAP、热休克转录因子和叉头蛋白的DNA结合结构域相似，尽管它们之间没有序列同源性。
