Coulocheri Stavroula A, Pigis Diomidis G, Papavassiliou Kostas A, Papavassiliou Athanasios G
Department of Biological Chemistry, Medical School, University of Athens, Athens, Greece.
Biochimie. 2007 Nov;89(11):1291-303. doi: 10.1016/j.biochi.2007.07.020. Epub 2007 Jul 31.
Recognition of a DNA sequence by a protein is achieved by interface-coupled chemical and shape complementation. This complementation between the two molecules is clearly directional and is determined by the specific chemical contacts including mainly hydrogen bonds. Directionality is an instrumental property of hydrogen bonding as it influences molecular conformations, which also affects DNA-protein recognition. The prominent elements in the recognition of a particular DNA sequence by a protein are the hydrogen-bond donors and acceptors of the base pairs into the grooves of the DNA that must interact with complementary moieties of the protein partner. Protein side chains make most of the crucial contacts through bidentate and complex hydrogen-bonding interactions with DNA base edges hence conferring remarkable specificity.
蛋白质对DNA序列的识别是通过界面耦合的化学互补和形状互补来实现的。这两个分子之间的这种互补显然是有方向性的，并且由主要包括氢键在内的特定化学接触所决定。方向性是氢键的一个重要特性，因为它影响分子构象，而分子构象又会影响DNA-蛋白质识别。蛋白质识别特定DNA序列的主要因素是碱基对的氢键供体和受体进入DNA凹槽，这些凹槽必须与蛋白质伴侣的互补部分相互作用。蛋白质侧链通过与DNA碱基边缘的双齿和复杂氢键相互作用形成了大部分关键接触，从而赋予了显著的特异性。
