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Phosphorylated RPA32 (pRPA32) binds to RPA70 and perchance regulates the transient RPA70-Bloom syndrome helicase (BLM) interaction to prevent DNA resection. But, the architectural details and determinants associated with the phosphorylated RPA32-RPA70 communication continue to be unidentified. In this study, we provide molecular information on the communication between RPA70 and a mimic of phosphorylated RPA32 (pmRPA32) using fluorescence polarization and NMR e