Sandbox I3DC Try 2

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(New page: <StructureSection load='' size='450' side='right' scene='10/1081088/007_fig_02_new/4' caption='Crystal structure of TβRI–SB505124 complex 9f6x showing the ICD Kinase domain (blue) a...)
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<StructureSection load='' size='450' side='right' scene='10/1081088/007_fig_02_new/4' caption='Crystal structure of TβRI–SB505124 complex [[9f6x]] showing the ICD Kinase domain (blue) and SB505124, as spheres with CPK colors, occupying the ATP binding cleft betwf6x]] een the kinase N- and C-lobes.'>
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<StructureSection load='' size='450' side='right' scene='10/1081089/007_fig_02_new/1' caption='Crystal structure of TβRI–SB505124 complex [[9f6x]] showing the ICD Kinase domain (blue) and SB505124, as spheres with CPK colors, occupying the ATP binding cleft betwf6x]] een the kinase N- and C-lobes.'>
===Human TGFβR1 in complex with kinase inhibitor SB505124===
===Human TGFβR1 in complex with kinase inhibitor SB505124===
<big>Jhon A. Rodriguez Buitrago, Marene Landstrom, Magnus Wolf-Watz</big> <ref>PMID:39441620</ref>
<big>Jhon A. Rodriguez Buitrago, Marene Landstrom, Magnus Wolf-Watz</big> <ref>PMID:39441620</ref>
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<b>Molecular Tour</b><br>
<b>Molecular Tour</b><br>
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This study presents the high-resolution crystal structure of the intracellular domain of <scene name='10/1081088/007_fig_02_new/4'>TGFβR1 in complex with the competitive inhibitor SB505124</scene>. The 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.
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This study presents the high-resolution crystal structure of the intracellular domain of <scene name='10/1081089/007_fig_02_new/1'>TGFβR1 in complex with the competitive inhibitor SB505124</scene>. The 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 <scene name='10/1060550/Fig_02/2'>interactions between TGFβR1 and SB505124</scene>, offering a comprehensive view of how this inhibitor binds to and affects the receptor's conformation. A comparison of the ICD–SB505124 and ICD–SB431542 complexes is seen in a <scene name='10/1060550/007_fig_3_new_01_png/2'>close-up view</scene>.
1. Structural Insights: We reveal the atomic-level <scene name='10/1060550/Fig_02/2'>interactions between TGFβR1 and SB505124</scene>, offering a comprehensive view of how this inhibitor binds to and affects the receptor's conformation. A comparison of the ICD–SB505124 and ICD–SB431542 complexes is seen in a <scene name='10/1060550/007_fig_3_new_01_png/2'>close-up view</scene>.

Revision as of 15:17, 20 May 2025

Crystal structure of TβRI–SB505124 complex 9f6x showing the ICD Kinase domain (blue) and SB505124, as spheres with CPK colors, occupying the ATP binding cleft betwf6x]] een the kinase N- and C-lobes.

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