Saudek V, Pastore A, Castiglione Morelli M A, Frank R, Gausepohl H, Gibson T, Weih F, Roesch P
Merrell Dow Research Institute, Strasbourg, France.
Protein Eng. 1990 Oct;4(1):3-10. doi: 10.1093/protein/4.1.3.
The solution structure of an active synthetic peptide containing both the leucine zipper and the adjacent basic domain of the yeast transcription factor GCN4 (residues 220-280) was determined by NMR. The two domains show structurally distinct behaviours. In the absence of DNA, the basic domain is, although very flexible, structured and fluctuating around a helical conformation. The leucine zipper region forms a long, uninterrupted helix. From a suitable set of NMR distances the three-dimensional structure of the leucine zipper monomeric sub-domain was calculated by distance geometry algorithms. The structure of the symmetrical parallel dimer was obtained by model building using the NMR information. A smaller peptide with the sequence of the isolated basic region (residues 1-35 of the 61 residue peptide) was also synthesized. Circular dichroism studies showed 30-40% helicity. A flexible helix spans the region between residues 8 and 21. The comparison of our results with suggested models is discussed in detail.
通过核磁共振（NMR）确定了一种活性合成肽的溶液结构，该肽包含酵母转录因子GCN4的亮氨酸拉链和相邻的碱性结构域（第220 - 280位氨基酸残基）。这两个结构域表现出结构上不同的行为。在没有DNA的情况下，碱性结构域虽然非常灵活，但具有结构且围绕螺旋构象波动。亮氨酸拉链区域形成一个长的、不间断的螺旋。通过距离几何算法从一组合适的NMR距离计算出亮氨酸拉链单体亚结构域的三维结构。利用NMR信息通过模型构建获得对称平行二聚体的结构。还合成了一个具有分离碱性区域序列（61个氨基酸残基的肽中的第1 - 35位氨基酸残基）的较小肽。圆二色性研究表明其螺旋度为30 - 40%。一个灵活的螺旋跨越第8位和第21位氨基酸残基之间的区域。详细讨论了我们的结果与建议模型的比较。
