A global transcription cofactor bound to juxtaposed strands of unwound DNA

被引：40

作者：

Werten, S ^{[1
]}

Moras, D ^{[1
]}

机构：

[1] Inst Genet & Biol Mol & Cellulaire, Dept Biol & Genom Struct, F-67404 Illkirch Graffenstaden, France

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2006年 / 13卷 / 02期

关键词：

D O I：

10.1038/nsmb1044

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 1.74-angstrom crystal structure of the human transcription cofactor PC4 in complex with a single-stranded 20-mer oligonucleotide reveals how symmetry-related beta-surfaces of the protein homodimer interact with juxtaposed 5-nucleotide DNA regions running in opposite directions. The structure explains high-affinity binding of PC4 to the complementary strands of unwinding duplex DNA, and it suggests the cofactor may have a role in relaxing negative supercoils or exposing unpaired bases for sequence-specific recognition by other biomolecules.

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页码：181 / 182

页数：2

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