Institute for Molecular Science and Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, Myodaiji, Okazaki, Japan.
FEBS Lett. 2013 Jun 5;587(11):1605-9. doi: 10.1016/j.febslet.2013.04.007. Epub 2013 Apr 18.
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.
在这里，我们报告了一项使用淀粉样 β (Aβ) 作为模型配体的 GroEL 底物相互作用模式的 NMR 研究。我们发现 GroEL 可以通过与 Aβ(1-40) 的两个疏水区段 Leu17-Ala21 和 Ala30-Val36 相互作用来抑制其淀粉样形成，这两个疏水区段涉及纤丝形成的关键残基。Aβ(1-40) 的结合位点被映射到位于 GroEL 顶端域的一对α-螺旋上。这些结果为伴侣蛋白对病理相关淀粉样蛋白的识别提供了新的见解。
