Electrostatics and flexibility in protein-DNA interactions.
Electrostatics and flexibility in protein-DNA interactions.
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DOI：
10.1016/0065-227x(85)90034-6
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发表时间：
1985-01-01
影响因子：
--
通讯作者：
Matthew, J B
中科院分区：
文献类型：
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作者：
Ohlendorf, D H;Matthew, J B
CAP、cro和lambda阻遏因子代表一类基因调控蛋白，它们通过共同的双螺旋基序特异性地与DNA结合。对这些结构的检查提示了蛋白质与DNA结合的可能机制。第一步是形成非特异性的蛋白质-DNA复合体，这种复合体是由蛋白质表面不对称分布的电荷的静电相互作用能量驱动的，这些电荷补充了DNA上的电荷。这种吸引力使蛋白质靠近DNA，将扩散限制在一个维度上。当蛋白质滑动时，随机的热波动扭曲并使蛋白质浸入DNA结构的不规则结构中。在这些漫游过程中，对表面互补性进行采样，直到找到特定的结合位点。在这一点上，中间溶剂被置换，使两个分子的静电和氢键相互作用最大化。
CAP, cro, and lambda repressor represent a class of gene-regulatory proteins that bind specifically to DNA using a common bihelical motif. Examination of these structures suggest a possible mechanism for the binding of protein to DNA. The first step would be the formation of a non-specific protein-DNA complex energetically driven by the electrostatic interaction of asymetrically distributed charges on the surface of the protein that complement the charges on DNA. This attraction keeps the protein near the DNA, limiting diffusion to one dimension. As the protein slides, random thermal fluctuations twist and dip the protein over irregularities in the structure of the DNA. During these excursions, surface complementarity is sampled until the specific binding site is found. At this point the intervening solvent is displaced allowing the two molecules maximize their electrostatic and hydrogen bonding interactions.