Kelch-like protein

Function

Kelch-like proteins (KLHL) contain multiple Kelch motifs. This motif is about 50 residues long and forms a four-stranded β-sheet blade. Six to Eight such blades form a circular β-propeller domain. β-prepellers are involved in protein-protein interactions. The N-terminal of KLHL contains other protein domains like BTB (Broad-Tramtrack-Bric-a-brac) which is also involved in protein-protein interactions^[1].

Disease

Relevance

KLHL19 (Keap1) interacts with the Neh2 peptide of NRF2. NRF2 is a regulator of antioxidant response, hence Keap1 is investigated as a drug target.

Structural highlights