Abstract: More specifically, conversion of
glutamic acid 143 to arginine within TM4 severely reduced 16K/
E5 binding, suggesting that charged interactions facilitated efficient binding.
Abstract: This hypothesis was confirmed by demonstrating that binding to the defective 16K arginine mutant could be restored by complementary charge mutations in
E5; conversion of
E5 glutamine 17 to glutamic acid or aspartic acid enhanced interactions with the 16K arginine mutant.