Journal:Acta Cryst F:S2053230X24010094

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2. Regulatory Mechanisms: Our structural analysis sheds light on the functional implications of SB505124 binding, particularly its role in disrupting TGF-β signaling pathways, which are often deregulated in various cancers.
2. Regulatory Mechanisms: Our structural analysis sheds light on the functional implications of SB505124 binding, particularly its role in disrupting TGF-β signaling pathways, which are often deregulated in various cancers.
3. Therapeutic Potential: Based on our structural findings, we discuss the potential of SB505124 as a therapeutic agent in cancer treatment, providing a foundation for future drug development efforts targeting TGFβR1.
3. Therapeutic Potential: Based on our structural findings, we discuss the potential of SB505124 as a therapeutic agent in cancer treatment, providing a foundation for future drug development efforts targeting TGFβR1.
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<b>References</b><br>
<b>References</b><br>
<references/>
<references/>
</StructureSection>
</StructureSection>
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Revision as of 16:52, 27 October 2024

Crystal structure of TβRI–SB505124 complex showing the ICD Kinase domain (blue) and SB505124, as spheres with CPK colors, occupying the ATP binding cleft between the kinase N- and C-lobes.

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