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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Atomic structure of a tryptophan-zipper pentamer.
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Atomic structure of a tryptophan-zipper pentamer.

机译：色氨酸拉链五聚体的原子结构。

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摘要

Coiled-coil motifs are ubiquitous mediators of specific protein-protein interactions through the formation of interlocking hydrophobic seams between alpha-helical chains. Residues that form these seams occur at the first (a) and fourth (d) positions of a characteristic 7-aa repeat and are primarily aliphatic. The potential of aromatic residues to promote helix association in a coiled coil was explored by engineering a "Trp-zipper" protein with Trp residues at all 14 a and d positions. The protein forms a discrete, stable, alpha-helical pentamer in water at physiological pH. Its 1.45-A crystal structure reveals a parallel, five-stranded coiled coil, a previously uncharacterized type of "knobs-into-holes" packing interaction between interfacial Trp side chains, and an unusual approximately 8-A-diameter axial channel lined with indole rings that is filled with polyethylene glycol 400 and water and sulfate ion molecules. The engineered Trp-zipper pentamer enlarges current views of coiled-coil assembly, molecular recognition, and protein engineering, and may serve as a soluble model for membrane ion channels.
机译：螺旋线圈基元是通过α-螺旋链之间互锁的疏水接缝形成的特定蛋白质-蛋白质相互作用的普遍介体。形成这些接缝的残基出现在特征性7-aa重复序列的第一（a）和第四（d）位置，主要为脂肪族。通过工程改造在所有14个a和d位带有Trp残基的“ Trp-zipper”蛋白，探索了芳香族残基在卷曲螺旋中促进螺旋缔合的潜力。该蛋白质在生理pH值下在水中形成离散，稳定的α-螺旋五聚体。它的1.45-A晶体结构揭示了一个平行的五链盘绕线圈，界面Trp侧链之间以前没有特征的“旋钮-入孔”堆积相互作用以及不寻常的大约8-A直径的轴向通道衬有吲哚环充满聚乙二醇400，水和硫酸根离子分子。工程设计的Trp-zipper五聚体扩大了盘绕线圈组装，分子识别和蛋白质工程的当前视野，并且可以用作膜离子通道的可溶模型。

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