https://www.selleckchem.com/pr....oducts/bay-11-7082-b
The K64Q mutation results in altered binding profiles with the highest binding affinity to PIP(4,5)P2 with specific acyl chains. Mutation of R92 to Pro, a residue found in Kir6.2, results in promiscuous binding of PIP isoforms. Kir3.2 with the K194A mutation results in a distinct binding preference for PIP(3,4,5)P3 over other PIP isoforms. Taken together, our results underscore the utmost importance of protein quality for protein-lipid binding studies and a single mutation in Kir3.2 can alter the selectivity toward PIPs.
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