Structural Determinants of Transmembrane Helical Proteins
Structural Determinants of Transmembrane Helical Proteins
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DOI：
10.1016/j.str.2009.06.009
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发表时间：
2009-08-12
期刊：
影响因子：
5.7
通讯作者：
Ben-Tal, Nir
中科院分区：
文献类型：
--
作者：
Harrington, Susan E.;Ben-Tal, Nir
我们确定了跨膜螺旋蛋白的结构特征，限制了它们的构象空间，并提出了一种新的方式来理解其天然状态的构建和稳定性。我们发现，五种众所周知的特定的有利的螺旋间的相互作用（氢键，芳族相互作用，盐桥，和两个相互作用从包装图案）精确地确定包装的跨膜螺旋在15个不同的蛋白质。为了证明这一点，我们迭代重组的螺旋束的每种蛋白质只使用这些相互作用，通用的相互作用的几何形状，和个人的螺旋骨架构象。平均而言，最好地满足由五种类型的螺旋间相互作用施加的约束的重建结构的代表性集合具有与1.03埃的原生的平均C α均方根偏差。蛋白质折叠，结构和运动预测，建模和设计的影响进行了讨论。
We identify a structural feature of transmembrane helical proteins that restricts their conformational space and suggests a new way of understanding the construction and stability of their native states. We show that five kinds of well-known specific favorable interhelical interactions (hydrogen bonds, aromatic interactions, salt bridges, and two interactions from packing motifs) precisely determine the packing of the transmembrane helices in 15 diverse proteins. To show this, we iteratively reassemble the helix bundle of each protein using only these interactions, generic interaction geometries, and individual helix backbone conformations. On average, the representative set of rebuilt structures best satisfying the constraints imposed by the five types of interhelical interactions has an average C alpha root-mean-square deviation from the native of 1.03 angstrom. Implications for protein folding, structure and motion prediction, modeling, and design are discussed.