Berman H M, Neidle S, Zimmer C, Thrum H
Biochim Biophys Acta. 1979 Jan 26;561(1):124-31. doi: 10.1016/0005-2787(79)90496-9.
The crystal structure of netropsin, an oligopeptide which binds to DNA, has been determined. The molecule is bowed with the amide groups on the concave side, and the carbonyl and methyl groups on the convex side. The amide groups participate in extensive hydrogen bonding with water molecules; the charged amino end groups interact with the sulfate anions. Binding of netropsin to poly(dA) . poly(dT) under conditions of different ionic strength was also studied. Utilizing the crystallographic as well as the binding data, it is possible to build a model which explains the specificity of this antibiotic.
已确定与DNA结合的寡肽纺锤菌素的晶体结构。该分子呈弓形,酰胺基团位于凹面,羰基和甲基位于凸面。酰胺基团与水分子广泛形成氢键;带电荷的氨基端基团与硫酸根阴离子相互作用。还研究了在不同离子强度条件下纺锤菌素与聚(dA)·聚(dT)的结合。利用晶体学数据和结合数据,可以构建一个解释这种抗生素特异性的模型。