Human TGFβR1 in complex with kinase inhibitor SB505124
Jhon A. Rodriguez Buitrago, Marene Landstrom, Magnus Wolf-Watz [1]
Molecular Tour
This study presents the high-resolution crystal structure of the intracellular domain of T. 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:
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.
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.
References
- ↑ Rodriguez Buitrago JA, Landström M, Wolf-Watz M. Human transforming growth factor β type I receptor in complex with kinase inhibitor SB505124. Acta Crystallogr F Struct Biol Commun. 2024 Nov 1. PMID:39441620 doi:10.1107/S2053230X24010094
