CRYSTAL-STRUCTURE OF THE HETERODIMERIC BZIP TRANSCRIPTION FACTOR C-FOS-C-JUN BOUND TO DNA
CRYSTAL-STRUCTURE OF THE HETERODIMERIC BZIP TRANSCRIPTION FACTOR C-FOS-C-JUN BOUND TO DNA
复制标题
DOI：
10.1038/373257a0
复制
发表时间：
1995-01-19
期刊：
影响因子：
64.8
通讯作者：
HARRISON, SC
中科院分区：
文献类型：
--
作者：
GLOVER, JNM;HARRISON, SC
真核转录因子的FOS和Jun家族异源二聚化形成能够结合5 '-TGAGTCA-3' DNA元件的复合物。我们已经确定了异源二聚体的bZIP区域的c-Fos和c-Jun结合到DNA的X-射线晶体结构。两个亚基形成连续的α-螺旋。羧基末端区域形成不对称卷曲螺旋，氨基末端区域与大沟中的DNA进行碱基特异性接触。两种晶体学上不同的蛋白质-DNA复合物的比较显示卷曲螺旋柔性地连接到碱性区域，并且Fos-Jun异二聚体不识别独特取向的不对称5 '-TGAGTCA-3'识别元件。卷曲螺旋内的亚基之间存在广泛的静电相互作用网络，这与这些相互作用决定异二聚体优先形成于同二聚体的提议一致。
THE FOS and Jun families of eukaryotic transcription factors heterodimerize to form complexes capable of binding 5'-TGAGTCA-3' DNA elements. We have determined the X-ray crystal structure of a heterodimer of the bZIP regions of c-Fos and c-Jun bound to DNA. Both subunits form continuous alpha-helices. The carboxy-terminal regions form an asymmetric coiled-coil, and the amino-terminal regions make base-specific contacts with DNA in the major groove. Comparison of the two crystallographically distinct protein-DNA complexes show that the coiled-coil is flexibly joined to the basic regions and that the Fos-Jun heterodimer does not recognize the asymmetric 5'-TGAGTCA-3' recognition element in a unique orientation. There is an extensive network of electrostatic interactions between subunits within the coiled-coil, consistent with proposals that these interactions determine preferential formation of the heterodimer over either of the homodimers.