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首页> 外文期刊>Journal of Molecular Biology >Simultaneous formation of right- and left-handed anti-parallel coiled-coil interfaces by a coil2 fragment of human lamin A.
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Simultaneous formation of right- and left-handed anti-parallel coiled-coil interfaces by a coil2 fragment of human lamin A.

机译：人类层粘连蛋白A的coil2片段同时形成左右手反平行的盘绕线圈界面。

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摘要

The elementary building block of all intermediate filaments (IFs) is a dimer featuring a central alpha-helical rod domain flanked by the N- and C-terminal end domains. In nuclear IF proteins (lamins), the rod domain consists of two coiled-coil segments, coil1 and coil2, that are connected by a short non-helical linker. Coil1 and the C-terminal part of coil2 contain the two highly conserved IF consensus motifs involved in the longitudinal assembly of dimers. The previously solved crystal structure of a lamin A fragment (residues 305-387) corresponding to the second half of coil2 has yielded a parallel left-handed coiled coil. Here, we present the crystal structure and solution properties of another human lamin A fragment (residues 328-398), which is largely overlapping with fragment 305-387 but harbors a short segment of the tail domain. Unexpectedly, no parallel coiled coil forms within the crystal. Instead, the alpha-helices are arranged such that two anti-parallel coiled-coil interfaces are formed. The most significant interface has a right-handed geometry, which is accounted for by a characteristic 15-residue repeat pattern that overlays with the canonical heptad repeat pattern. The second interface is a left-handed anti-parallel coiled coil based on the predicted heptad repeat pattern. In solution, the fragment reveals only a weak dimerization propensity. We speculate that the C-terminus of coil2 might unzip, thereby allowing for a right-handed coiled-coil interface to form between two laterally aligned dimers. Such an interface might co-exist with a heterotetrameric left-handed coiled-coil assembly, which is expected to be responsible for the longitudinal A(CN) contact.
机译：所有中间丝（IF）的基本组成部分是二聚体，其特征是中央α-螺旋杆结构域与N和C末端域相连。在核IF蛋白（核纤层蛋白）中，棒结构域由两个盘绕的线圈段（线圈1和线圈2）组成，它们通过短的非螺旋接头连接。线圈1和线圈2的C端部分包含与二聚体的纵向装配有关的两个高度保守的IF共有基序。先前解析的与线圈2的后半部分相对应的层状A片段（残基305-387）的晶体结构产生了一个平行的左手线圈。在这里，我们介绍了另一个人类lamin A片段（残基328-398）的晶体结构和溶液性质，该片段与片段305-387大部分重叠，但尾部结构域很短。出乎意料的是，晶体中没有形成平行的线圈。取而代之的是，排列α螺旋，以便形成两个反平行的螺旋线圈界面。最重要的界面具有惯用右手的几何形状，这是由特征性的15残基重复序列所组成的，该重复序列与规范的庚烷重复序列重叠。第二个接口是基于预测的七pt重复模式的左手反平行盘绕线圈。在溶液中，该片段仅显示出弱的二聚化倾向。我们推测线圈2的C端可能会解压缩，从而允许在两个横向对齐的二聚体之间形成右旋线圈线圈界面。这样的界面可能与异四聚体左旋螺旋线圈组件共存，该组件有望引起纵向A（CN）接触。

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