Opposites Attract: Shape and Electrostatic Complementarity in Protein-DNA Complexes
Opposites Attract: Shape and Electrostatic Complementarity in Protein-DNA Complexes
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DOI：
10.1039/9781849735056-00053
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发表时间：
2012-01-01
期刊：
影响因子：
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通讯作者：
Fenley, Marcia Oliveira
中科院分区：
文献类型：
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作者：
Harris, Robert C.;Mackoy, Travis;Fenley, Marcia Oliveira
蛋白质-DNA结合在基因调控（通过高度特异性的转录因子-DNA相互作用）和染色质组织（通过组蛋白和其他结构蛋白与DNA的非特异性相互作用）中都起着关键作用。这一生物学重要性激发了蛋白质- dna结合的结构知识的迅速扩展，从x射线晶体学和核磁共振光谱数据中衍生出来
Protein-DNA binding plays a key role in both gene regulation–through highly specific transcription factor-DNA interactions–and in chromatin organization, through the largely non-specific interactions of histones and other architectural proteins with DNA. 1 This biological importance has inspired the rapid expansion in structural knowledge of protein-DNA binding, derived from X-ray crystallographic and NMR spectroscopic data, 2 ever since