NMR characterization of theinteraction of GroEL with amyloid ? as a model ligand.
 

NMR characterization of theinteraction of GroEL with amyloid ? as a model ligand.

Related Articles NMR characterization of theinteraction of GroEL with amyloid ? as a model ligand.

FEBS Lett. 2013 Apr 18;

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

Abstract
Here we report an NMR study on the substrate interaction modes of GroEL using amyloid?(A?) as a model ligand. We found that GroEL could suppress A?(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 A?(1-40) wasmapped on a pair of ?-helices located in the GroEL apical domain. These resultsprovide insights intochaperonin recognition of amyloidogenic proteins of pathological interest. STRUCTURED SUMMARY OF PROTEIN INTERACTIONS: A?(1-40)andA?(1-40)bindbyfluorescence technology(View interaction) A?(1-40)andA?(1-40)bindbynuclear magnetic resonance(View interaction) GroELandA?(1-40)bindbynuclear magnetic resonance(View interaction).


PMID: 23603391 [PubMed - as supplied by publisher]



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