Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

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

Yagi-Utsumi M., Kunihara T., Nakamura T., Uekusa Y., Makabe K., Kuwajima K., Kato K.

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.

FEBS Lett. 587:1605-1609(2013) [PubMed] [Europe PMC]

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health