Structural insight into an ankyrin-sensitive lipid-binding site of erythroid β-spectrin
Structural insight into an ankyrin-sensitive lipid-binding site of erythroid β-spectrin
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DOI：
10.1080/09687860601102427
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发表时间：
2007-01-01
影响因子：
--
通讯作者：
Sikorski, Aleksander F.
中科院分区：
文献类型：
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作者：
Czogalla, Aleksander;Jaszewski, Adrian R.;Sikorski, Aleksander F.
最近的研究表明，β-血影蛋白中负责与锚蛋白相互作用的区域包括一个脂结合部位，该部位对锚蛋白的抑制敏感。我们构建了一系列单自旋和双自旋标记的β-幽灵蛋白衍生肽，并通过电子顺磁共振波谱和傅里叶反卷积方法分析了它们的自旋-自旋距离，从而研究了它的结构。结果表明，β-血影蛋白对锚蛋白敏感的整个脂质结合部位呈现螺旋构象，在其N-末端有明显的310个螺旋的贡献。与理论预测相比，螺旋的起始位置位于序列上游的五个残基。基于所获得数据的模型提供了直接证据，证明所检查的脂结合位点是一个高度两亲性的螺旋，它与其N-末端片段的特定构象相关。
It was recently shown that the region within beta-spectrin responsible for interactions with ankyrin includes a lipid-binding site which displayed sensitivity to inhibition by ankyrin. We studied its structure by constructing a series of single and double spin-labeled beta-spectrin-derived peptides and analyzing their spin-spin distances via electron paramagnetic resonance spectroscopy and the Fourier deconvolution method. The results indicate that the whole ankyrin-sensitive lipid-binding site of beta-spectrin exhibits a helical conformation revealing a distinct 310-helix contribution at its N-terminus. The start of the helix was located five residues upstream along the sequence compared to the theoretical predictions. A model based on the obtained data provides direct evidence that the examined lipid-binding site is a highly amphipathic helix, which is correlated with the specific conformation of its N-terminal fragment.