Department of Chemistry, Lewis & Clark College, Portland, Oregon, USA.
Department of Biochemistry and Biophysics, Oregon State University, Corvallis, Oregon, USA.
Protein Sci. 2021 May;30(5):1056-1063. doi: 10.1002/pro.4055. Epub 2021 Mar 9.
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.
Swallow 是一种 62kDa 的多功能蛋白，对于几个在果蝇卵母细胞发育中涉及的 mRNA 的正确定位是必需的。Swallow 的二聚化依赖于蛋白质序列中心的一个 71 个残基的自组装结构域，并且与动力蛋白轻链（LC8）的结合相互作用显著稳定。在这里，我们详细介绍了使用溶液态核磁共振波谱法来对该自组装结构域的结构进行特征分析，从而证实了该结构域形成了一个平行的卷曲螺旋，并提供了对二聚化相互作用稳定性如何受到调节的深入了解。
