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Crystal structures of DCAF1-PROTAC-WDR5 ternary complexes provide insight into DCAF1 substrate specificity

The authors show that DCAF1, a substrate receptor of CUL4 and EDVP E3 ligases, can be recruited by PROTACs to degrade the cancer drug target, WDR5. They also report the crystal structures of PROTAC ternary complexes that reveal a significant role for loops in DCAF1 substrate recognition, a potential mechanism behind the diverse substrate specificity of DCAF1.

Mark F. Mabanglo
Brian Wilson
Masoud Vedadi
ResearchOpen Access23 Nov 2024
Nature Communications

Volume: 15, P: 1-17
OICR-41103 as a chemical probe for the DCAF1 WD40 domain

OICR-41103 is a potent, selective probe targeting the DCAF1 WDR domain and displacing viral Vpr protein. It enables new opportunities in cancer research, antiviral therapy, and targeted protein degradation via PROTACs.

Serah W. Kimani
Mahmoud Noureldin
Levon Halabelian
ResearchOpen Access19 Jul 2025
Communications Biology

Volume: 8, P: 1-12
The SUV4-20 inhibitor A-196 verifies a role for epigenetics in genomic integrity

SUV4-20 members mediate the di- and trimethylation of lysine 20 on histone H4. A chemical screen led to the identification of A-196 as a potent and selective inhibitor of SUV4-20 that decreases H4K20 methylation and alters DNA damage response.

Kenneth D Bromberg
Taylor R H Mitchell
William N Pappano
Research23 Jan 2017
Nature Chemical Biology

Volume: 13, P: 317-324
The co-crystal structure of Cbl-b and a small-molecule inhibitor reveals the mechanism of Cbl-b inhibition

Structural and biophysical characterization of a small molecule binding to Cbl-b E3 ligase reveals an intramolecular glue mechanism locking the protein in an inactive state.

Serah W. Kimani
Sumera Perveen
Levon Halabelian
ResearchOpen Access16 Dec 2023
Communications Biology

Volume: 6, P: 1-10
CACHE (Critical Assessment of Computational Hit-finding Experiments): A public–private partnership benchmarking initiative to enable the development of computational methods for hit-finding

Critical Assessment of Computational Hit-finding Experiments (CACHE) is a public benchmarking project to compare and improve computational small-molecule hit-finding approaches through cycles of prediction, compound synthesis and experimental testing. By that, CACHE will enable a more efficient and effective approach to hit identification and drug discovery.

Suzanne Ackloo
Rima Al-awar
Timothy M. Willson
Reviews15 Feb 2022
Nature Reviews Chemistry

Volume: 6, P: 287-295
Discovery of Nedd4 auto-ubiquitination inhibitors

Darren Yong
Stuart R. Green
Masoud Vedadi
ResearchOpen Access25 Sept 2023
Scientific Reports

Volume: 13, P: 1-15

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Crystal structures of DCAF1-PROTAC-WDR5 ternary complexes provide insight into DCAF1 substrate specificity

OICR-41103 as a chemical probe for the DCAF1 WD40 domain

The SUV4-20 inhibitor A-196 verifies a role for epigenetics in genomic integrity

The co-crystal structure of Cbl-b and a small-molecule inhibitor reveals the mechanism of Cbl-b inhibition

CACHE (Critical Assessment of Computational Hit-finding Experiments): A public–private partnership benchmarking initiative to enable the development of computational methods for hit-finding

Discovery of Nedd4 auto-ubiquitination inhibitors

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