Structural diversity in the small heat shock protein superfamily: control of aggregation by the N-terminal region.
Structural diversity in the small heat shock protein superfamily: control of aggregation by the N-terminal region.
复制标题
小热休克蛋白超家族的结构多样性：N 末端区域对聚集的控制。
DOI：
10.1093/protein/gzg102
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发表时间：
2003
期刊：
影响因子：
--
通讯作者：
Koretz,JaneF
中科院分区：
文献类型：
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作者：
Salerno,JohnC;Eifert,CherylL;Salerno,KathleenM;Koretz,JaneF
小的热休克蛋白超家族，延伸到所有王国，其特征在于具有可变的N-和C-末端延伸的共同核心结构域。相对疏水的N末端在促进和控制高级聚集中起着关键作用，这是超家族内高度结构变异的原因。使用嵌合蛋白和截短蛋白研究了N末端体积对聚集的影响。缺乏N-末端区域的蛋白质不会在四聚体上方聚集，而较大的N-末端导致大的聚集体，这与聚集体内部的N-末端包装一致。延伸内环的变异将典型的原核和植物超家族成员与它们的动物对应物区分开来;这意味着高阶聚集体的二聚体构建块的几何结构不同。
The small heat shock protein superfamily, extending over all kingdoms, is characterized by a common core domain with variable N‐ and C‐terminal extensions. The relatively hydrophobic N‐terminus plays a critical role in promoting and controlling high‐order aggregation, accounting for the high degree of structural variability within the superfamily. The effects of N‐terminal volume on aggregation were studied using chimeric and truncated proteins. Proteins lacking the N‐terminal region did not aggregate above the tetramers, whereas larger N‐termini resulted in large aggregates, consistent with the N‐termini packing inside the aggregates. Variation in an extended internal loop differentiates typical prokaryotic and plant superfamily members from their animal counterparts; this implies different geometry in the dimeric building block of high‐order aggregates.