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NMR characterization of the interaction of GroEL with amyloid β as a model ligand
Author(s) -
Yagi-Utsumi Maho,
Kunihara Tomoko,
Nakamura Takashi,
Uekusa Yoshinori,
Makabe Koki,
Kuwajima Kunihiro,
Kato Koichi
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.04.007
Subject(s) - groel , chaperonin , amyloid (mycology) , ligand (biochemistry) , chemistry , biophysics , amyloid fibril , crystallography , protein folding , biochemistry , amyloid β , biology , receptor , medicine , escherichia coli , pathology , gene , inorganic chemistry , disease
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.