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首页> 美国卫生研究院文献>other >Coiled-Coils at the Edge of Configurational Heterogeneity. Structural Analyses of Parallel and Antiparallel Homotetrameric Coiled-Coils Reveal Configurational Sensitivity to a Single Solvent-Exposed Amino Acid Substitution.
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Coiled-Coils at the Edge of Configurational Heterogeneity. Structural Analyses of Parallel and Antiparallel Homotetrameric Coiled-Coils Reveal Configurational Sensitivity to a Single Solvent-Exposed Amino Acid Substitution.

机译：构型异质性边缘处的卷材线圈。平行和反平行同四聚体卷曲螺旋的结构分析揭示了对单一溶剂暴露的氨基酸取代的构型敏感性。

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摘要

A detailed understanding of the mechanisms by which particular amino acid sequences can give rise to more than one folded structure, such as for proteins that undergo large conformational changes or misfolding, is a long-standing objective of protein chemistry. Here we describe the crystal structures of a single coiled-coil peptide in distinct parallel and antiparallel tetrameric configurations and further describe the parallel or antiparallel crystal structures of several related peptide sequences; the antiparallel tetrameric assemblies represents the first crystal structures of GCN4-derived peptides exhibiting such a configuration. Intriguingly, substitution of a single solvent-exposed residue enabled the parallel coiled-coil tetramer GCN4-pLI to populate the antiparallel configuration, suggesting that the two configurations are close enough in energy for subtle sequence changes to have important structural consequences. We present a structural analysis of the small changes to helix register and side chain conformations that accommodate the two configurations, and have supplemented these results using solution studies and a molecular dynamics energetic analysis using a replica exchange methodology. Considering the previous examples of structural nonspecificity in coiled-coil peptides, the findings reported here not only emphasize the predisposition of the coiled-coil motif to adopt multiple configurations, but also call attention to the associated risk that observed crytstal structures may not represent the only (or even the major) species present in solution.
机译：对特定氨基酸序列可以产生不止一个折叠结构的机制（例如经历大的构象变化或错误折叠的蛋白质）的详细理解是蛋白质化学的长期目标。在这里，我们描述了具有不同平行和反平行四聚体构型的单个卷曲螺旋肽的晶体结构，并进一步描述了几个相关肽序列的平行或反平行晶体结构。反平行四聚体组装体代表具有这种构型的GCN4衍生肽的第一晶体结构。有趣的是，单个暴露于溶剂的残基的取代使平行卷曲螺旋四聚体GCN4-pLI能够构成反平行构型，这表明这两种构型在能量上足够接近，对于细微的序列改变会产生重要的结构后果。我们提出了结构适应性的变化，以适应两个构型的螺旋结构和侧链构象的微小变化，并使用溶液研究和使用副本交换方法的分子动力学能量分析对这些结果进行了补充。考虑到卷曲螺旋肽中结构非特异性的先前实例，此处报道的发现不仅强调了卷曲螺旋基序倾向于采用多种构型，而且还引起人们注意观察到的晶体结构可能不代表唯一的相关风险。 （甚至主要）物种存在于溶液中。

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