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首页> 外文期刊>Journal of Molecular Biology >Terminal Regions Confer Plasticity to the Tetrameric Assembly of Human HspB2 and HspB3
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Terminal Regions Confer Plasticity to the Tetrameric Assembly of Human HspB2 and HspB3

机译：终端区域赋予人Hspb2和Hspb3的四聚体组装的可塑性

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Heterogeneity in small heat shock proteins (sHsps) spans multiple spatiotemporal regimes-from fast fluctuations of part of the protein, to conformational variability of tertiary structure, plasticity of the interfaces, and polydispersity of the inter-converting, and co-assembling oligomers. This heterogeneity and dynamic nature of sHsps has significantly hindered their structural characterization. Atomic coordinates are particularly lacking for vertebrate sHsps, where most available structures are of extensively truncated homomers. sHsps play important roles in maintaining protein levels in the cell and therefore in organismal health and disease. HspB2 and HspB3 are vertebrate sHsps that are found co-assembled in neuromuscular cells, and variants thereof are associated with disease. Here, we present the structure of human HspB2/B3, which crystallized as a hetero-tetramer in a 3:1 ratio. In the HspB2/B3 tetramer, the four alpha-crystallin domains (ACDs) assemble into a flattened tetrahedron which is pierced by two non-intersecting approximate dyads. Assembly is mediated by flexible "nuts and bolts" involving IXI/N motifs from terminal regions filling ACD pockets. Parts of the N-terminal region bind in an unfolded conformation into the anti-parallel shared ACD dimer grooves. Tracts of the terminal regions are not resolved, most likely due to their disorder in the crystal lattice. This first structure of a full-length human sHsp heteromer reveals the heterogeneous interactions of the terminal regions and suggests a plasticity that is important for the cytoprotective functions of sHsps. (C) 2018 The Authors. Published by Elsevier Ltd.
机译：小型热休克蛋白（SHSP）中的异质性跨越多个时空制度 - 从一部分蛋白质的快速波动，构成三级结构的可变性，界面的互联性，以及相互转换间的多分散性和共组装的低聚物。 SHSP的这种异质性和动态性质显着阻碍了它们的结构表征。脊椎动物SHSP特别缺乏原子坐标，其中最可获得的结构是广泛的截断的均方。 SHSP在维持细胞中的蛋白质水平并因此发挥重要作用，因此在有机体健康和疾病中。 HSPB2和HSPB3是发现在神经肌肉细胞中共组合的脊椎动物SHSP，并且其变体与疾病有关。这里，我们介绍了人Hspb2 / b3的结构，其在3：1的比例中作为杂 - 四聚体结晶。在HSPB2 / B3四聚体中，四个α-晶体域（ACD）组装成扁平的四面体，其被两个非交叉近似二元刺穿。组件由柔性“螺母和螺栓”介导，涉及来自填充ACD口袋的端子区域的IXI / N图谱。 N末端区域的部分在展开的构象中绑定到抗并联共享ACD二聚体槽中。终端区域的椎间没有解决，很可能是由于它们在晶格中的疾病。全长人SHSP异构体的第一结构揭示了终端区域的异质相互作用，并表明了SHSP的细胞保护功能重要的可塑性。 （c）2018年作者。 elsevier有限公司出版

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