X-Ray Structure of the GCN4 Leucine Zipper, a Two-Stranded, Parallel Coiled Coil

作者：Erin K. O’Shea, Juli D. Klemm, Peter S. Kim, Tom Alber · 发表于：Science · 年份：1991 · DOI：10.1126/science.1948029 · 被引用次数：1459 · 研究领域：Genomics and Chromatin Dynamics、Enzyme Structure and Function、RNA and protein synthesis mechanisms

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.