NMR characterization of interaction of GroEL with amyloid β as a model ligand.
NMR characterization of interaction of GroEL with amyloid β as a model ligand.
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GroEL 与淀粉样蛋白 β 作为模型配体相互作用的 NMR 表征。
DOI：
10.1016/j.febslet.2013.04.007
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发表时间：
2013
期刊：
影响因子：
--
通讯作者：
and K.Kato
中科院分区：
文献类型：
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作者：
M.Yagi-Utsumi;T.Kunihara;T.Nakamura;Y.Uekusa;K.Makabe;K.Kuwajima;and K.Kato
本文报道了以淀粉样蛋白β（Aβ）为模型配体对GroEL底物相互作用模式的NMR研究。我们发现GroEL可以通过与其两个疏水片段Leu 17-Ala 21和Ala 30-Val 36相互作用来抑制Aβ（1-40）淀粉样蛋白的形成，这两个疏水片段涉及原纤维形成的关键残基。Aβ（1-40）的结合位点位于GroEL顶端结构域的一对α-螺旋上。这些结果提供了深入了解伴侣蛋白识别淀粉样蛋白的病理利益。
Here we report an NMR study on the substrate interaction modes of GroEL using amyloid β (Aβ) as a model ligand. We found that GroEL could suppress Aβ(1–40) amyloid formation by interacting with its two hydrophobic segments Leu17-Ala21 and Ala30-Val36, which involve key residues in fibril formation. The binding site of Aβ(1–40) was mapped on a pair of α-helices located in the GroEL apical domain. These results provide insights into chaperonin recognition of amyloidogenic proteins of pathological interest.