Abstract：
Glucose-regulated protein 78 (GRP78), also termed HSPA5, was widely studied in cancer. It was recently approved that GRP78 has nuclear localization potential that sheds light on its role in cancer development. The inhibitor of DNA binding and differentiation 2 (ID2) is the nuclear component that associates with GRP78. The interaction between these two proteins is not understood clearly. In the current study, the binding pattern of GRP78/ID2 is predicted using computational methods. Protein-protein docking is used along with molecular dynamics simulation. The substrate binding domain β of GRP78 can stably interact with the loop region (C42-S60) of ID2 as predicted in this study. This paves the way for a possible destabilizer for this association and cancer eradication.
摘要：
葡萄糖调节蛋白78(GRP78),也称为HSPA5，在癌症中被广泛研究。最近批准GRP78具有核定位潜力，这揭示了其在癌症发展中的作用。DNA结合和分化2（ID2）的抑制剂是与GRP78相关的核成分。这两种蛋白质之间的相互作用尚不清楚。在目前的研究中,GRP78/ID2的结合模式是使用计算方法预测的。蛋白质-蛋白质对接与分子动力学模拟一起使用。GRP78的底物结合结构域β可以稳定地与ID2的环区(C42-S60)相互作用,如本研究中所预测的。这为这种关联和癌症根除的可能的去稳定剂铺平了道路。
