Crystal structure and assembly of a eukaryotic small heat shock protein
Crystal structure and assembly of a eukaryotic small heat shock protein
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DOI：
10.1038/nsb722
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发表时间：
2001-12-01
期刊：
影响因子：
--
通讯作者：
Vierling, E
中科院分区：
文献类型：
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作者：
van Montfort, RLM;Basha, E;Vierling, E
小麦HSP 16.9是小分子热休克蛋白（small heat shock proteins，sHSPs）的成员之一，其2.7 bp的结构表明其α-晶体蛋白结构域及其侧翼延伸部分是如何组装成一个十二聚体双盘的。单体的折叠和寡聚体的组装是相互依赖的，涉及链交换、螺旋交换、松散结和铰链延伸。为支持分子伴侣机制，底物结合的二聚体在温度依赖性平衡中具有更高的组装形式，具有未折叠的N-末端臂并暴露α-晶状体蛋白结构域上的保守疏水结合位点。该结构还提供了一种模型，通过该模型，sHSP蛋白家族的成员结合未折叠的底物，这些底物参与各种神经退行性疾病和白内障形成。
The 2.7 Å structure of wheat HSP16.9, a member of the small heat shock proteins (sHSPs), indicates how its α-crystallin domain and flanking extensions assemble into a dodecameric double disk. The folding of the monomer and assembly of the oligomer are mutually interdependent, involving strand exchange, helix swapping, loose knots and hinged extensions. In support of the chaperone mechanism, the substrate-bound dimers, in temperature-dependent equilibrium with higher assembly forms, have unfolded N-terminal arms and exposed conserved hydrophobic binding sites on the α-crystallin domain. The structure also provides a model by which members of the sHSP protein family bind unfolded substrates, which are involved in a variety of neurodegenerative diseases and cataract formation.