Sandbox I3DC 007

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(New page: ==Your Heading Here (maybe something like 'Structure')== <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> This is a default text for you...)
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==Your Heading Here (maybe something like 'Structure')==
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<StructureSection load='' size='350' side='right' scene='10/1060550/Fig_02/1' caption='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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<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
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===Human TGFβR1 in complex with kinase inhibitor SB505124===
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This is a default text for your page '''Sandbox I3DC 007'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
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<big>Jhon A. Rodriguez Buitrago, Marene Landstrom, Magnus Wolf-Watz</big> <ref>PMID:39441620</ref>
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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
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<hr/>
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<b>Molecular Tour</b><br>
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== Function ==
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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>. 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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The manuscript highlights several key points:
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== Disease ==
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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>.
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2. Regulatory Mechanisms: The 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.
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== Relevance ==
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3. Therapeutic Potential: Based on the structural findings, the potential of SB505124 as a therapeutic agent in cancer treatment is discussed, providing a foundation for future drug development efforts targeting TGFβR1.
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<br>
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== Structural highlights ==
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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<b>References</b><br>
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<references/>
</StructureSection>
</StructureSection>
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== References ==
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<references/>
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Revision as of 13:33, 20 May 2025

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.

Drag the structure with the mouse to rotate
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