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Updated: Mar 21, 2026

Author Spotlight: Integrating BRET-Based Assays and Rare Mutation Analysis to Decipher RAF Kinase Regulation in Live Cells
Published on: March 1, 2024
Pranlukast, a novel binding ligand of human Raf1 kinase inhibitory protein
Tao Sun1, Zhihua Wu1, Mengyao Luo1
1Department of Chemical Biology, College of Chemistry and Chemical Engineering, Xiamen University, 422 Siming South Road, Xiamen, 361005, Fujian, China.
Objectives:
To study the binding of pranlukast to hRKIP and its regulatory role in the Raf1/MEK/ERK signal pathway.
Results:
NMR and fluorescence experiments demonstrated hRKIP could bind pranlukast with a binding constant of 1016 mM(-1). Residues (Y81, S109 and Y181) on the conserved ligand-binding pocket of hRKIP played a crucial role in binding pranlukast, and their mutations reduced the binding affinity more than 85 %. Furthermore, 25 μM pranlukast could up-regulate the ERK phosphorylation by about 17 %.
Conclusion:
Pranlukast may be used as a potential drug precursor for treating hRKIP involved diseases.
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