Structural characterization of the self-association domain of swallow.
Structural characterization of the self-association domain of swallow.
复制标题
燕子自关联域的结构表征。
DOI：
10.1002/pro.4055
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发表时间：
2021
期刊：
影响因子：
--
通讯作者：
Barbar,Elisar
中科院分区：
文献类型：
--
作者：
Loening,NikolausM;Barbar,Elisar
Swallow是一种62kda的多结构域蛋白，是果蝇卵母细胞发育过程中几种mrna的正确定位所必需的。Swallow的二聚化依赖于蛋白序列中心的71个残基自结合结构域，并通过与动力蛋白轻链（LC8）的结合相互作用显着稳定。在这里，我们详细使用溶液态核磁共振波谱来表征这种自结合结构域的结构，从而确定该结构域形成一个平行的卷曲线圈，并提供了如何调节二聚化相互作用的稳定性的见解。
Swallow, a 62 kDa multidomain protein, is required for the proper localization of several mRNAs involved in the development of Drosophila oocytes. The dimerization of Swallow depends on a 71‐residue self‐association domain in the center of the protein sequence, and is significantly stabilized by a binding interaction with dynein light chain (LC8). Here, we detail the use of solution‐state nuclear magnetic resonance spectroscopy to characterize the structure of this self‐association domain, thereby establishing that this domain forms a parallel coiled‐coil and providing insight into how the stability of the dimerization interaction is regulated.