O'Shea E K, Klemm J D, Kim P S, Alber T
Howard Hughes Medical Institute, Cambridge, MA 02142.
Science. 1991 Oct 25;254(5031):539-44. doi: 10.1126/science.1948029.
The x-ray crystal structure of a peptide corresponding to the leucine zipper of the yeast transcriptional activator GCN4 has been determined at 1.8 angstrom resolution. The peptide forms a parallel, two-stranded coiled coil of alpha helices packed as in the "knobs-into-holes" model proposed by Crick in 1953. Contacts between the helices include ion pairs and an extensive hydrophobic interface that contains a distinctive hydrogen bond. The conserved leucines, like the residues in the alternate hydrophobic repeat, make side-to-side interactions (as in a handshake) in every other layer of the dimer interface. The crystal structure of the GCN4 leucine zipper suggests a key role for the leucine repeat, but also shows how other features of the coiled coil contribute to dimer formation.
已在1.8埃分辨率下确定了与酵母转录激活因子GCN4亮氨酸拉链相对应的肽段的X射线晶体结构。该肽段形成了一个平行的、由α螺旋组成的双链卷曲螺旋结构，其堆积方式如同1953年克里克提出的“旋钮入孔”模型。螺旋之间的接触包括离子对和一个广泛的疏水界面，该界面包含一个独特的氢键。保守的亮氨酸，就像交替疏水重复序列中的残基一样，在二聚体界面的每隔一层中进行侧向相互作用（如同握手）。GCN4亮氨酸拉链的晶体结构表明亮氨酸重复序列起着关键作用，但同时也展示了卷曲螺旋的其他特征是如何促进二聚体形成的。
