NMR characterization of the interaction of GroEL with amyloid β as a model ligand

Maho Yagi-Utsumi, Tomoko Kunihara, Takashi Nakamura, Yoshinori Uekusa, Koki Makabe, Kunihiro Kuwajima, Koichi Kato

研究成果: Article査読

15 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)1605-1609
ページ数5
ジャーナルFEBS Letters
587
11
DOI
出版ステータスPublished - 2013 6 5
外部発表はい

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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