Lys(199) mutation of the human angiotensin type 1 receptor differentially affects the binding of surmountable and insurmountable non-peptide antagonists.

@article{Fierens2000Lys199MO,
  title={Lys(199) mutation of the human angiotensin type 1 receptor differentially affects the binding of surmountable and insurmountable non-peptide antagonists.},
  author={Frederik L. P. Fierens and Patrick M. L. Vanderheyden and Zsuzsanna G{\'a}borik and Tran Minh and J P Backer and L{\'a}szl{\'o} Hunyady and Ad P. Ijzerman and Georges Vauquelin},
  journal={Journal of the renin-angiotensin-aldosterone system : JRAAS},
  year={2000},
  volume={1 3},
  pages={283-8}
}
Many slow dissociating (insurmountable) non-peptide angiotensin type 1 receptor (AT1) antagonists contain,besides the acidic biphenyltetrazole substructure of losartan, a second acidic group to stabilise antagonist-receptor complexes. To investigate the involved basic amino-acids of the human AT1-receptor, wild-type and mutant receptors were transiently transfected in CHO-K1 cells and characterised by [3H]candesartan binding. Lys199-->Gln substitution decreased the affinity 45-fold for… CONTINUE READING