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

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)1605-1609
Number of pages5
JournalFEBS Letters
Volume587
Issue number11
DOIs
Publication statusPublished - 2013 Jun 5

Keywords

  • Amyloid β
  • Chaperonin
  • GroEL
  • NMR
  • NOE

ASJC Scopus subject areas

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

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  • Cite this

    Yagi-Utsumi, M., Kunihara, T., Nakamura, T., Uekusa, Y., Makabe, K., Kuwajima, K., & Kato, K. (2013). NMR characterization of the interaction of GroEL with amyloid β as a model ligand. FEBS Letters, 587(11), 1605-1609. https://doi.org/10.1016/j.febslet.2013.04.007