The Structure and Topology of α-Helical Coiled Coils.
The Structure and Topology of α-Helical Coiled Coils.
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DOI：
10.1007/978-3-319-49674-0_4
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发表时间：
2017
影响因子：
--
通讯作者：
Dunin-Horkawicz S
中科院分区：
文献类型：
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作者：
Lupas AN;Bassler J;Dunin-Horkawicz S
α-螺旋卷曲线圈构成了迄今为止描述的最多样化的折叠之一。它们的长度范围超过两个数量级；它们形成杆、分段绳、桶、漏斗、片、螺旋和环，其中包含两个到超过 20 个平行或反平行方向的螺旋；它们具有不同的螺旋交叉角、超螺旋程度和堆积几何形状。这种结构多样性支持广泛的生物功能，使它们能够形成机械刚性结构，为分子马达提供杠杆，长距离投射域，介导寡聚化，转导构象变化并促进其他分子的运输。与我们所知的几乎任何其他蛋白质折叠不同，它们的结构可以通过参数方程计算，使它们成为合理蛋白质设计的理想模型系统。在这里，我们概述了卷绕线圈的构造原理，回顾了其折叠和稳定性的决定因素，并概述了其不同的架构。
α-Helical coiled coils constitute one of the most diverse folds yet described. They range in length over two orders of magnitude; they form rods, segmented ropes, barrels, funnels, sheets, spirals, and rings, which encompass anywhere from two to more than 20 helices in parallel or antiparallel orientation; they assume different helix crossing angles, degrees of supercoiling, and packing geometries. This structural diversity supports a wide range of biological functions, allowing them to form mechanically rigid structures, provide levers for molecular motors, project domains across large distances, mediate oligomerization, transduce conformational changes and facilitate the transport of other molecules. Unlike almost any other protein fold known to us, their structure can be computed from parametric equations, making them an ideal model system for rational protein design. Here we outline the principles by which coiled coils are structured, review the determinants of their folding and stability, and present an overview of their diverse architectures.