Disulfide bridges in extracellular domains of angiotensin II receptor type IA.

@article{Ohyama1995DisulfideBI,
  title={Disulfide bridges in extracellular domains of angiotensin II receptor type IA.},
  author={Kenji Ohyama and Yoshiaki Yamano and Takeshi Sano and Yoshiko Nakagomi and Takao Hamakubo and Isao Morishima and Tadashi Inagami},
  journal={Regulatory peptides},
  year={1995},
  volume={57 2},
  pages={141-7}
}
Angiotensin II receptor type IA (AT1A) has a cysteine (Cys) residue in each of four extracellular domains, and these Cys residues are believed to form two disulfide bridges. However, the question as to which pairs of Cys residues form disulfide bridges have not been experimentally determined. We constructed four mutants of rat AT1A, in which extracellular Cys residues were individually replaced by glycine (mutant C-1, C-2, C-3 and C-4). Further, we constructed two double mutants, in which two… CONTINUE READING

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CysteineNo subtypeGlycine
We constructed four mutants of rat AT1A , in which extracellular Cys residues were individually replaced by glycine ( mutant C-1 , C-2 , C-3 and C-4 ) .
Further , we constructed two double mutants , in which two extracellular Cys residues were simultaneously substituted for by glycine .
GlycineNo subtypeCysteine
We constructed four mutants of rat AT1A , in which extracellular Cys residues were individually replaced by glycine ( mutant C-1 , C-2 , C-3 and C-4 ) .
Further , we constructed two double mutants , in which two extracellular Cys residues were simultaneously substituted for by glycine .
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