Scripps Research identifies binding site on challenging cancer protein

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Scripps Research identifies binding site on challenging cancer protein
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Hormone-driven cancers, like those of the breast and prostate, often rely on a tricky-to-target protein called Forkhead box protein 1 (FOXA1). FOXA1 mutations can enable these types of cancers to grow and proliferate.

Scripps Research InstituteOct 15 2024 Hormone -driven cancers, like those of the breast and prostate, often rely on a tricky-to-target protein called Forkhead box protein 1 . FOXA1 mutations can enable these types of cancers to grow and proliferate. Today, FOXA1 is notoriously difficult to block with drugs-;but that may soon change.

FOXA1 had historically been considered undruggable. It's thought to lack the types of surfaces that small molecule drugs can bind to, which is likely why it's been so difficult to target the protein." Following its discovery, Cravatt's lab teamed up with the lab of Michael Erb, PhD, to better understand how those molecules might affect the functions of FOXA1.

Related Stories"FOXA1 is a master regulator of gene control, or what we call a lineage-defining factor," says Erb, the study's co-corresponding author and an associate professor in the Department of Chemistry. "We found a specific site on FOXA1 that can bind to small molecules, which is a tremendously important discovery since transcription factors like FOXA1 are not only attractive targets for cancer, but also many other diseases.

Another surprising finding: FOXA1 usually binds to a distinct sequence of DNA bases to control gene regulation-;but binding FOXA1 to small molecules changed the sequences that it preferred, allowing the protein to target different genes than it normally would. Furthermore, the team determined that certain mutations in FOXA1 affected areas close to where small molecules could attach to the protein. These mutations changed how FOXA1 interacted with DNA-;in the exact same way that the small molecules did.

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