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• W2890591443 abstract "SUMMARY BTB-Kelch proteins form the largest subfamily of Cullin-RING E3 ligases, yet their substrate complexes are mapped and structurally characterized only for KEAP1 and KLHL3. KLHL20 is a related CUL3-dependent ubiquitin ligase linked to autophagy, cancer and Alzheimer’s disease that promotes the ubiquitination and degradation of substrates including DAPK1, PML and ULK1. We identified a ‘LPDLV’-containing recruitment site in the DAPK1 death domain and determined the 1.1 Å crystal structure of a KLHL20-DAPK1 complex. DAPK1 binds to KLHL20 as a loose helical turn that inserts deeply into the central pocket of the Kelch domain to contact all six blades of the β-propeller. Here, KLHL20 forms a salt bridge as well as hydrophobic interactions that include a tryptophan and cysteine residue ideally positioned for covalent inhibitor development. The structure highlights the diverse binding modes of circular substrate pockets versus linear grooves and suggests a novel E3 ligase for protac-based drug design." @default.
• W2890591443 created "2018-09-27" @default.
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• W2890591443 date "2018-09-12" @default.
• W2890591443 modified "2023-10-17" @default.
• W2890591443 title "Structural basis for recruitment of DAPK1 to the KLHL20 E3 ligase" @default.
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• W2890591443 doi "https://doi.org/10.1101/414250" @default.
• W2890591443 hasPublicationYear "2018" @default.
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