X-RAY STRUCTURE OF THE GCN4 LEUCINE ZIPPER, A 2-STRANDED, PARALLEL COILED COIL
X-RAY STRUCTURE OF THE GCN4 LEUCINE ZIPPER, A 2-STRANDED, PARALLEL COILED COIL
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DOI：
10.1126/science.1948029
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发表时间：
1991-10-25
期刊：
影响因子：
56.9
通讯作者：
ALBER, T
中科院分区：
文献类型：
--
作者：
OSHEA, EK;KLEMM, JD;ALBER, T
已在1.8埃分辨率下测定了对应于酵母转录激活因子GCN 4的亮氨酸拉链的肽的X射线晶体结构。该肽形成一个平行的双链卷曲螺旋，α螺旋如克里克在1953年提出的“节入孔”模型中所述。螺旋之间的接触包括离子对和包含独特氢键的广泛疏水性界面。保守的亮氨酸，像交替疏水重复中的残基一样，在二聚体界面的每一层中进行侧对侧的相互作用（如握手）。GCN 4亮氨酸拉链的晶体结构表明了亮氨酸重复的关键作用，但也显示了卷曲螺旋的其他特征如何有助于二聚体的形成。
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.