YPEL3 that induces cellular senescence in both normal and tumour cells of humans may show altered expression under the influence of incidental mutations. In this study, we proposed the first structure of Native YPEL3 protein and its five possible deleterious mutants—V40M, C61Y, G98R, G108S, and A131T and predicted their deleterious effects to alter stability, flexibility and conformational changes in the protein. The MD simulation (RMSD, RMSF, Rg, h-bond and SASA) analysis revealed that the variants V40M, G98R and G108S increased the flexibility in protein, and variant V40M imparted more compactness to the protein.. In general, variants attributed changes in the native conformation and structure of the YPEL3 protein which might affect the native function of cellular senescence. The study provides opportunities for health professionals and practitioners in formulating précised medicines to effectively cure various cancers. We propose in-vitro or in-vivo studies should consider these reported nsSNPs while examining any malfunction in the YPEL3 protein.

在人类正常细胞和肿瘤细胞中诱导细胞衰老的 YPEL3 可能在偶然突变的影响下表现出改变的表达。在这项研究中，我们提出了天然 YPEL3 蛋白的第一个结构及其五种可能的有害突变体——V40M、C61Y、G98R、G108S 和 A131T，并预测了它们对改变蛋白质稳定性、灵活性和构象变化的有害影响。MD 模拟（RMSD、RMSF、Rg、h-bond 和 SASA）分析显示变体 V40M、G98R 和 G108S 增加了蛋白质的灵活性，变体 V40M 赋予蛋白质更多的紧凑性。 YPEL3 蛋白的天然构象和结构可能会影响细胞衰老的天然功能。该研究为卫生专业人员和从业人员提供了制定有效治疗各种癌症的精准药物的机会。我们建议体外或体内研究在检查 YPEL3 蛋白中的任何故障时应考虑这些报告的 nsSNP。