Kelch-like protein
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ContentsFunctionKelch-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-propellers 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].
DiseaseSomatic mutations in Keap1 were found in lung cancer patients. RelevanceNRF2 is a regulator of antioxidant response, hence Keap1 is investigated as a drug target. Structural highlightsThe interaction of Keap1 with Neh2 is through the first Glu in the latter's ETGE motif[2]. All interactions of Keap1 with Neh2. Water molecules shown as red spheres. 3D Structures of Kelch-like proteinKelch-like protein 3D structures
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This page was last modified 09:56, 8 September 2019.