Journal:Acta Cryst F:S2053230X24010094
From Proteopedia
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<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
| - | This study presents the high-resolution crystal structure of the intracellular domain of | + | This study presents the high-resolution crystal structure of the intracellular domain of T<scene name='10/1060550/Fig_02/1'>GFβR1 in complex with the competitive inhibitor SB505124</scene>. Our findings provide detailed insights into this complex's molecular interactions and structural configuration, elucidating the mechanisms by which SB505124 inhibits TGFβR1 activity. These insights are significant for understanding the regulation of TGF-β signaling, a pathway critically involved in cancer biology. |
The manuscript highlights several key points: | The manuscript highlights several key points: | ||
1. Structural Insights: We reveal the atomic-level interactions between TGFβR1 and SB505124, offering a comprehensive view of how this inhibitor binds to and affects the receptor's conformation. | 1. Structural Insights: We reveal the atomic-level interactions between TGFβR1 and SB505124, offering a comprehensive view of how this inhibitor binds to and affects the receptor's conformation. | ||
Revision as of 12:50, 22 October 2024
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