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茯苓中麦角-7，22E-二烯-3β-醇的靶点蛋白PRGR的结构分析与功能预测
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贵州轻工职业大学， 贵州 贵安 561116

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黔教合KY字［2016］332；贵州省科技支撑重点项目（黔科合支撑001）。


Structural Analysis and Functional Prediction of PRGR, a Target Protein of the Poria Ergosta-7,22E-dien-3β-ol
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Guizhou Light Industry Polytechnic University, Guian 561116, China

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    摘要:

    【目的】应用生物信息学和分子对接方法研究茯苓甾醇类活性成分麦角-7，22E-二烯-3β-醇与孕激素受体（PRGR）的互作机制及其潜在的治疗作用。【方法】利用TCMSP数据库筛选茯苓的有效成分，使用MEGA X（10.0.5）对PRGR蛋白序列进行多重比对，通过ProtParam分析PRGR蛋白的一级结构，Protscale预测PRGR蛋白的疏水性，Prosite分析PRGR蛋白的氨基酸序列，通过NPS @ SOPMA网站分析PRGR蛋白的二级结构，运用RCSB PDB数据库结合同源建模方法预测PRGR蛋白的三级结构，通过DeepLoc-2.0网站预测PRGR蛋白的亚细胞定位，运用SwissDock网站对茯苓有效成分麦角-7，22E-二烯-3β-醇与其潜在靶点孕激素受体（3O5Q）进行分子对接验证。【结果】PRGR蛋白由933个氨基酸组成，相对分子质量98 980，理论等电点6.09，属于亲水性不稳定蛋白质；其二级结构以无规卷曲（占比70.31%）为主，并含有核受体配体结合域（NR LBD）及C4型锌指结构，提示其在核信号传导中的核心功能。麦角-7，22E-二烯-3β-醇通过疏水相互作用及氢键锚定于PRGR配体结合口袋，关键结合位点涉及亮氨酸（Leu）、丙氨酸（Ala）等残基。PRGR在灵长类中高度保守，与人类亲缘关系最近的物种（黑猩猩、倭黑猩猩）分支值达98%以上；PRGR可能通过细胞核及线粒体外膜参与免疫调控，分子对接显示麦角-7，22E-二烯-3β-醇与PRGR蛋白可能形成稳定的复合物。【结论】阐明了茯苓中甾醇类成分与PRGR的分子结合机制，为靶向PRGR的免疫调节药物开发及药食同源资源的精准利用提供理论支撑，同时为天然产物-核受体互作研究提供新思路。

    Abstract:

    [Objective]This study aims to investigate the mechanism of the interaction between ergosta-7,22E-dien-3β-ol, an active sterol of Poria, and progesterone receptor (PRGR) and the potential therapeutic effects via bioinformatics and molecular docking.[Method]The TCMSP database was used to screen the active ingredients of Poria, and MEGA X (10.0.5) was used for alignment of multiple PRGR sequences. The primary structure of PRGR was analyzed by ProtParam, and the hydrophobicity of PRGR was predicted by Protscale. The amino acid sequence of PRGR was analyzed by Prosite, and the secondary structure of PRGR was analyzed on NPS@SOPMA. The RCSB PDB database was used to predict the tertiary structure of PRGR via the homologous modeling method. DeepLoc-2.0 website was used to predict the subcellular localization of PRGR. SwissDock was employed to simulate the molecular docking between ergosta-7,22E-diene-3β-ol and its potential target PRGR (3O5Q).[Result]The PRGR protein consisted of 933 amino acid residues, with a relative molecular mass of 98 980 and a theoretical isoelectric point of 6.09, being a hydrophilic unstable protein. Its secondary structure was dominated by random coils (70.31% of the total), and this protein contained nuclear receptor ligand-binding domains (NR LBDs) and C4-type zinc-finger structure, which suggested its core function in nuclear signaling. Ergosta-7,22E-dien-3β-ol was anchored to the PRGR ligand-binding pocket through hydrophobic interactions and hydrogen bonding, and the key binding sites involved residues such as Leu and Ala. PRGR was highly conserved in primates, with branching values of more than 98% in the species (chimpanzee and bonobo) with closest affinity to humans. PRGR may be involved in the immune regulation through the nucleus and the outer membrane of mitochondria. Molecular docking revealed that ergosta-7,22E-dien-3β-ol may form a stable complex with PRGR.[Conclusion]This study elucidates the molecular binding mechanism of a sterol in Poria with PRGR, providing theoretical support for the development of immunomodulatory drugs targeting PRGR and the precise utilization of resources with both medicinal and edible values. Meanwhile, this study provides new ideas for the research on natural product-nuclear receptor interactions.

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刘永飞,任艳玲,王涛,吴茂钊,彭婧,吴昌云,李泽秀.茯苓中麦角-7，22E-二烯-3β-醇的靶点蛋白PRGR的结构分析与功能预测[J].食品与生物技术学报,2025,(10):163-172.

LIU Yongfei, REN Yanling, WANG Tao, WU Maozhao, PENG Jing, WU Changyun, LI Zexiu. Structural Analysis and Functional Prediction of PRGR, a Target Protein of the Poria Ergosta-7,22E-dien-3β-ol[J]. Journal of Food Science and Biotechnology,2025,(10):163-172.

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  • 收稿日期:2025-03-06
  • 最后修改日期:2025-05-08
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  • 在线发布日期: 2026-01-14
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