Gursky A V, Tumanyan V G, Zasedatelev A S, Zhuze A L, Grokhovsky S L, Gottikh B P
Mol Biol Rep. 1976 Apr;2(5):413-25. doi: 10.1007/BF00366264.
A possible code is suggested that describes a correspondence between amino acid sequences in stereospecific sites of regulatory proteins and nucleotide sequences at the control sites on DNA. Stereospecific sites of regulatory proteins are assumed to contain pairs of antiparallel polypeptide chain segments which form a right-hand twisted antiparallel beta-sheet with single-stranded regions at the ends of the beta-structure. The binding reaction between regulatory protein and double-helical DNA is accompanied by significant structural alterations at stereospecific sites of the protein and DNA. Half of the hydrogen bonds normally existing in beta-structure are broken upon complex formation with DNA and a new set of hydrogen bonds is formed between polypeptide amide groups and DNA base pairs. The code states a correspondence between four amino acid residues at a stereospecific site of the regulatory protein and an AT (GC) base pair at the control site. It predicts that there are six fundamental amino acid residues (serine, threonine, histidine, asparagine, glutamine and cysteine) whose arrangement in the stereospecific site determines the base pair sequence to which a given regulatory protein would bind preferentially.
提出了一种可能的编码，它描述了调节蛋白立体特异性位点中的氨基酸序列与DNA上控制位点的核苷酸序列之间的对应关系。调节蛋白的立体特异性位点被认为包含反平行多肽链段对，这些链段形成右手扭曲的反平行β-折叠，在β-结构的末端有单链区域。调节蛋白与双螺旋DNA之间的结合反应伴随着蛋白质和DNA立体特异性位点的显著结构改变。与DNA形成复合物时，β-结构中通常存在的一半氢键会断裂，并且在多肽酰胺基团和DNA碱基对之间会形成一组新的氢键。该编码表明调节蛋白立体特异性位点的四个氨基酸残基与控制位点的一个AT（GC）碱基对之间的对应关系。它预测有六个基本氨基酸残基（丝氨酸、苏氨酸、组氨酸、天冬酰胺、谷氨酰胺和半胱氨酸），它们在立体特异性位点的排列决定了给定调节蛋白优先结合的碱基对序列。
