A new DNA-binding motif in the Skn-1 binding domain DNA complex

被引:48
作者
Rupert, PB
Daughdrill, GW
Bowerman, B
Matthews, BW [1 ]
机构
[1] Univ Oregon, Inst Mol Biol, Eugene, OR 97403 USA
[2] Univ Oregon, Howard Hughes Med Inst, Eugene, OR 97403 USA
[3] Univ Oregon, Dept Biol, Eugene, OR 97403 USA
[4] Univ Oregon, Dept Chem, Eugene, OR 97403 USA
[5] Univ Oregon, Dept Phys, Eugene, OR 97403 USA
关键词
D O I
10.1038/nsb0698-484
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The DNA-binding domain of Skn-1, a developmental transcription factor that specifies mesoderm in C. elegans, is shown by X-ray crystallography to have a novel fold in which a compact, monomeric, four-helix unit organizes two DNA-contact elements. At the C-terminus, a helix extends from the domain to occupy the major groove of DNA in a manner similar to bZip proteins. Skn-1, however, lacks the leucine zipper found in all bZips. Additional contacts with the DNA are made by a short basic segment at the N-terminus of the domain, reminiscent of the 'homeodomain arm'.
引用
收藏
页码:484 / 491
页数:8
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