Structural insights into human brachyury DNA recognition and discovery of progressible binders for cancer therapy

Abstract Brachyury is a transcription factor that plays an essential role in tumour growth of the rare bone cancer chordoma and is implicated in other solid tumours. Brachyury is minimally expressed in healthy tissues, making it a potential therapeutic target. Unfortunately, as a ligandless transcri...

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Main Authors: Joseph A. Newman, Angeline E. Gavard, Nergis Imprachim, Hazel Aitkenhead, Hadley E. Sheppard, Robert te Poele, Paul A. Clarke, Mohammad Anwar Hossain, Louisa Temme, Hans J. Oh, Carrow I. Wells, Zachary W. Davis-Gilbert, Paul Workman, Opher Gileadi, David H. Drewry
Format: Article
Language:English
Published: Nature Portfolio 2025-02-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-025-56213-1
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author Joseph A. Newman
Angeline E. Gavard
Nergis Imprachim
Hazel Aitkenhead
Hadley E. Sheppard
Robert te Poele
Paul A. Clarke
Mohammad Anwar Hossain
Louisa Temme
Hans J. Oh
Carrow I. Wells
Zachary W. Davis-Gilbert
Paul Workman
Opher Gileadi
David H. Drewry
author_facet Joseph A. Newman
Angeline E. Gavard
Nergis Imprachim
Hazel Aitkenhead
Hadley E. Sheppard
Robert te Poele
Paul A. Clarke
Mohammad Anwar Hossain
Louisa Temme
Hans J. Oh
Carrow I. Wells
Zachary W. Davis-Gilbert
Paul Workman
Opher Gileadi
David H. Drewry
author_sort Joseph A. Newman
collection DOAJ
description Abstract Brachyury is a transcription factor that plays an essential role in tumour growth of the rare bone cancer chordoma and is implicated in other solid tumours. Brachyury is minimally expressed in healthy tissues, making it a potential therapeutic target. Unfortunately, as a ligandless transcription factor, brachyury has historically been considered undruggable. To investigate direct targeting of brachyury by small molecules, we determine the structure of human brachyury both alone and in complex with DNA. The structures provide insights into DNA binding and the context of the chordoma associated G177D variant. We use crystallographic fragment screening to identify hotspots on numerous pockets on the brachyury surface. Finally, we perform follow-up chemistry on fragment hits and describe the progression of a thiazole chemical series into binders with low µM potency. Thus we show that brachyury is ligandable and provide an example of how crystallographic fragment screening may be used to target protein classes that are difficult to address using other approaches.
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spelling doaj-art-a2c3997617084185b9fb4b7f8a653c7e2025-08-20T02:43:11ZengNature PortfolioNature Communications2041-17232025-02-0116111410.1038/s41467-025-56213-1Structural insights into human brachyury DNA recognition and discovery of progressible binders for cancer therapyJoseph A. Newman0Angeline E. Gavard1Nergis Imprachim2Hazel Aitkenhead3Hadley E. Sheppard4Robert te Poele5Paul A. Clarke6Mohammad Anwar Hossain7Louisa Temme8Hans J. Oh9Carrow I. Wells10Zachary W. Davis-Gilbert11Paul Workman12Opher Gileadi13David H. Drewry14Centre for Medicines Discovery, University of OxfordCentre for Medicines Discovery, University of OxfordCentre for Medicines Discovery, University of OxfordCentre for Medicines Discovery, University of OxfordCentre for Cancer Drug Discovery, The Institute of Cancer ResearchCentre for Cancer Drug Discovery, The Institute of Cancer ResearchCentre for Cancer Drug Discovery, The Institute of Cancer ResearchSGC-UNC, University of North Carolina at Chapel HillSGC-UNC, University of North Carolina at Chapel HillSGC-UNC, University of North Carolina at Chapel HillSGC-UNC, University of North Carolina at Chapel HillSGC-UNC, University of North Carolina at Chapel HillCentre for Cancer Drug Discovery, The Institute of Cancer ResearchCentre for Medicines Discovery, University of OxfordSGC-UNC, University of North Carolina at Chapel HillAbstract Brachyury is a transcription factor that plays an essential role in tumour growth of the rare bone cancer chordoma and is implicated in other solid tumours. Brachyury is minimally expressed in healthy tissues, making it a potential therapeutic target. Unfortunately, as a ligandless transcription factor, brachyury has historically been considered undruggable. To investigate direct targeting of brachyury by small molecules, we determine the structure of human brachyury both alone and in complex with DNA. The structures provide insights into DNA binding and the context of the chordoma associated G177D variant. We use crystallographic fragment screening to identify hotspots on numerous pockets on the brachyury surface. Finally, we perform follow-up chemistry on fragment hits and describe the progression of a thiazole chemical series into binders with low µM potency. Thus we show that brachyury is ligandable and provide an example of how crystallographic fragment screening may be used to target protein classes that are difficult to address using other approaches.https://doi.org/10.1038/s41467-025-56213-1
spellingShingle Joseph A. Newman
Angeline E. Gavard
Nergis Imprachim
Hazel Aitkenhead
Hadley E. Sheppard
Robert te Poele
Paul A. Clarke
Mohammad Anwar Hossain
Louisa Temme
Hans J. Oh
Carrow I. Wells
Zachary W. Davis-Gilbert
Paul Workman
Opher Gileadi
David H. Drewry
Structural insights into human brachyury DNA recognition and discovery of progressible binders for cancer therapy
Nature Communications
title Structural insights into human brachyury DNA recognition and discovery of progressible binders for cancer therapy
title_full Structural insights into human brachyury DNA recognition and discovery of progressible binders for cancer therapy
title_fullStr Structural insights into human brachyury DNA recognition and discovery of progressible binders for cancer therapy
title_full_unstemmed Structural insights into human brachyury DNA recognition and discovery of progressible binders for cancer therapy
title_short Structural insights into human brachyury DNA recognition and discovery of progressible binders for cancer therapy
title_sort structural insights into human brachyury dna recognition and discovery of progressible binders for cancer therapy
url https://doi.org/10.1038/s41467-025-56213-1
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