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首页> 外文期刊>Journal of Molecular Biology >Structural polymorphism of oligomeric adiponectin visualized by electron microscopy.
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Structural polymorphism of oligomeric adiponectin visualized by electron microscopy.

机译：通过电子显微镜观察寡聚脂连蛋白的结构多态性。

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Adiponectin, a macromolecular complex similar to the members of the C1q and other collagenous homologues, elicits diverse biological functions, including anti-diabetes, anti-atherosclerosis, anti-inflammation and anti-tumor activities, which have been directly linked to the high molecular weight (HMW) oligomeric structures formed by multiples of adiponectin trimers. Here, we report the 3-D reconstructions of isolated full-length, recombinant murine C39A adiponectin trimer and hexamer of wild-type trimers (the major HMW form) determined by single-particle analysis of electron micrographs. The pleiomorphic ensemble of collagen-like stretches of the trimers leads to a dynamic structure of HMW that partition into two major classes, the fan-shaped (class I) and bouquet-shaped (class II). In both of these, while the N termini cluster into a compact ellipsoid-shaped (approximately 60 Ax45 Ax45 A) volume, the collagenous domains assume a variety of arrangements. The domains are splayed by up to approximately 90 degrees in class I, can form a close-packed, up to approximately 100x40 A cylindrical assembly in class II, which can house about half of the 66 putative collagen-like sequence and the rest, tethered to the trimeric globular domains at the C terminus, are highly dynamic. As a result, the globular domains elaborate a variety of arrangements, covering an area of up to approximately 4.9x10(5) A(2) and up to approximately 320 A apart, some of which were captured in reconstructions of class II. Our reconstructions suggest that the N-terminal structured domain, agreeing approximately with the expected volume for the octadecameric assembly of the terminal 27 amino acids, is crucial to the formation of the functionally active HMW. On the other hand, conformational flexibility of the trimers at the C terminus can allow the HMW to access and cluster disparate target ligands binding to the globular domains, which may be necessary to activate cellular signaling leading to the remarkable functional diversity of adiponectin.
机译：脂联素是类似于C1q和其他胶原同源物的大分子复合物，具有多种生物学功能，包括抗糖尿病，抗动脉粥样硬化，抗炎和抗肿瘤活性，这些都与高分子量直接相关。 （HMW）寡聚结构，由脂联素三聚体的倍数形成。在这里，我们报告通过电子显微照片的单颗粒分析确定的分离的全长重组鼠C39A脂联素三聚体和野生型三聚体（主要的HMW形式）的六聚体的3-D重建。三聚体的胶原状延伸的多态性集合导致HMW的动态结构，该结构分为两个主要类别，即扇形（I类）和花束形（II类）。在这两种情况下，N末端都簇成一个紧凑的椭圆形（大约60 Ax45 Ax45 A）体积，而胶原结构域则采取了多种排列方式。在I类中，这些域最多可扩展90度，可形成一个密排的，高达100x40的A类II圆柱体，可容纳约66个假定的胶原样序列的一半，而其余部分则被束缚在C末端的三聚球状结构域是高度动态的。结果，球状区域形成了各种排列方式，覆盖的面积最大约为4.9x10（5）A（2），最大相距约为320 A，其中一些是在II类的重建中捕获的。我们的重建表明，与末端27个氨基酸的十八聚体组装的预期体积大致相符的N末端结构域对功能性功能性HMW的形成至关重要。另一方面，三聚体在C末端的构象柔性可使HMW接近并聚集与球状结构域结合的完全不同的靶配体，这可能是激活细胞信号转导导致脂联素显着功能多样性所必需的。

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