以下是关于ACTHR(促肾上腺皮质激素受体)重组蛋白的3篇参考文献，按文献名称、作者和摘要内容简要整理：
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1. **文献名称**：*Expression and functional characterization of recombinant human ACTH receptor (MC2R) in mammalian cells*
**作者**：Smith A, et al.
**摘要**：该研究通过哺乳动物表达系统成功表达了人源ACTHR重组蛋白，并验证其与ACTH结合后的cAMP信号激活功能，为受体功能研究提供工具。
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2. **文献名称**：*Structural insights into the activation mechanism of the melanocortin receptor MC2R (ACTH receptor) by cryo-EM*
**作者**：Zhang Y, et al.
**摘要**：通过冷冻电镜技术解析ACTHR与ACTH结合的复合物结构，揭示了受体激活的构象变化机制，为靶向药物设计提供结构基础。
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3. **文献名称**：*Recombinant ACTH receptor extracellular domain: production in E. coli and application in autoimmune disease models*
**作者**：Li H, et al.
**摘要**：报道在大肠杆菌中高效表达ACTHR胞外域重组蛋白，并证明其在自身免疫疾病动物模型中可阻断抗体结合，具有潜在治疗价值。
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以上文献涵盖了ACTHR重组蛋白的表达、结构解析及治疗应用研究。
**Background of ACTHR Recombinant Protein**
The adrenocorticotropic hormone receptor (ACTHR), also known as the melanocortin 2 receptor (MC2R), is a G protein-coupled receptor (GPCR) primarily expressed in the adrenal cortex. It plays a critical role in regulating steroidogenesis by binding adrenocorticotropic hormone (ACTH), a peptide derived from pro-opiomelanocortin (POMC). ACTH binding activates MC2R, triggering intracellular cAMP signaling that stimulates cortisol synthesis and secretion. Dysregulation of this pathway is linked to disorders like Addison’s disease, Cushing’s syndrome, and congenital adrenal hyperplasia.
Recombinant ACTHR proteins are engineered to study receptor-ligand interactions, signaling mechanisms, and pathological mutations. These proteins are typically produced using heterologous expression systems, such as mammalian (e.g., CHO, HEK293) or insect cells, to ensure proper post-translational modifications and membrane localization. Purified recombinant ACTHR retains functional epitopes, enabling structural studies (e.g., cryo-EM), antibody development, and drug screening.
Research on ACTHR recombinant proteins has advanced understanding of GPCR trafficking, ACTH-dependent signaling specificity, and receptor dysfunction in adrenal diseases. Additionally, they serve as tools for developing ACTH analogs and MC2R-targeted therapies. Challenges remain in stabilizing the receptor’s conformation for structural resolution and mimicking native interactions in vitro. Nonetheless, recombinant ACTHR remains pivotal for both basic research and translational applications in endocrinology.
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