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<p>This dissertation presents a detailed investigation into the structural dynamics of P2X receptors, a group of ligand-gated ion channels activated by extracellular ATP. These receptors play a crucial role in a wide range of physiological processes, including neurotransmission, inflammation, and immune responses. The research focused on understanding the conformational changes that occur in P2X receptors, upon binding with ATP (Sheng in Proteins Struct Funct Bioinf 90(10):1779–1785, 2022). Through the use of advanced techniques such as AlphaFold 3 and structural alignment metrics like RMSD and TM-score, significant insights were gained into how ATP binding triggers transitions from closed to open and desensitized states in these receptors. Key findings from this research include the identification of conformational states that are essential for understanding the processes of receptor activation and desensitization. The importance of ATP in stabilizing the active states of these receptors is emphasized. By integrating structural predictions with functional implications, a comprehensive understanding of P2X receptor dynamics and their physiological roles has been achieved, this establishes the foundation for future investigations focused on experimental validation and drug discovery, underscoring the broader impact of P2X receptors in biomedical research.</p>

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Sampling the conformational states of P2X receptors with AlphaFold3

  • 期刊论文

  • 发表日期：

    2025年2月21日

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  • Amirhossein Soltani

摘要

This dissertation presents a detailed investigation into the structural dynamics of P2X receptors, a group of ligand-gated ion channels activated by extracellular ATP. These receptors play a crucial role in a wide range of physiological processes, including neurotransmission, inflammation, and immune responses. The research focused on understanding the conformational changes that occur in P2X receptors, upon binding with ATP (Sheng in Proteins Struct Funct Bioinf 90(10):1779–1785, 2022). Through the use of advanced techniques such as AlphaFold 3 and structural alignment metrics like RMSD and TM-score, significant insights were gained into how ATP binding triggers transitions from closed to open and desensitized states in these receptors. Key findings from this research include the identification of conformational states that are essential for understanding the processes of receptor activation and desensitization. The importance of ATP in stabilizing the active states of these receptors is emphasized. By integrating structural predictions with functional implications, a comprehensive understanding of P2X receptor dynamics and their physiological roles has been achieved, this establishes the foundation for future investigations focused on experimental validation and drug discovery, underscoring the broader impact of P2X receptors in biomedical research.