The Structure and Function of the PRMT5: MEP50 Complex
The Structure and Function of the PRMT5: MEP50 Complex
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DOI：
10.1007/978-3-319-46503-6_7
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发表时间：
2017-01-01
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影响因子：
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通讯作者：
Antonysamy, Stephen
中科院分区：
文献类型：
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作者：
Antonysamy, Stephen
蛋白精氨酸甲基转移酶 5 (PRMT5) 以组织特异性方式在细胞周期不同阶段的细胞过程中发挥多种作用。 PRMT5 与 MEP50/p44/WDR77 复合，与大量伙伴蛋白结合，对称地二甲基化细胞核和细胞质中靶蛋白上的精氨酸残基。在多种癌症中观察到 PRMT5 过度表达，使其成为有吸引力的药物靶点。与 S-腺苷甲硫氨酸类似物和底物肽结合的 453 kDa 杂八聚 PRMT5: MEP50 复合物的结构为了解这一有趣的靶标提供了宝贵的见解。
Protein arginine methyltransferase 5 (PRMT5) plays multiple roles in cellular processes at different stages of the cell cycle in a tissue specific manner. PRMT5 in complex with MEP50/p44/WDR77 associates with a plethora of partner proteins to symmetrically dimethylate arginine residues on target proteins in both the nucleus and the cytoplasm. Overexpression of PRMT5 has been observed in several cancers, making it an attractive drug target. The structure of the 453 kDa heterooctameric PRMT5: MEP50 complex bound to an S-adenosylmethionine analog and a substrate peptide provides valuable insights into this intriguing target.