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- W2078559904 abstract "G protein-coupled receptors (GPCRs) are the largest family of cell surface receptors and major targets for drug development. Herein, we sought to identify the regions of the human angiotensin II (AngII) type 1 (hAT1) receptor binding cleft that interact with all positions of the AngII using photoaffinity labeling. We conducted a complete iterative walk-through of the AngII sequence with either p-benzoyl-l-phenylalanine (Bpa) or p-[3-(trifluoromethyl)-3H-diazirin-3-yl]-l-phenylalanine (Tdf) to yield two series of eight photoreactive analogues. Pharmacological properties assessment of these sixteen analogues showed that the CAM receptor has a structure−activity relationship (SAR) more amenable to the amino acid substitutions at positions 1, 2, 3, and 5 of AngII than the WT receptor. Photoaffinity labeling of the CAM receptor with the selected analogues, which exhibit different but complementary photochemical properties, suggested that the AngII amino-terminus resides in a hydrophilic environment and interacts simultaneously with different regions of the hAT1 receptor, including several ectodomains." @default.
- W2078559904 created "2016-06-24" @default.
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- W2078559904 date "2010-02-10" @default.
- W2078559904 modified "2023-10-17" @default.
- W2078559904 title "The Amino-Terminus of Angiotensin II Contacts Several Ectodomains of the Angiotensin II Receptor AT<sub>1</sub>" @default.
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- W2078559904 doi "https://doi.org/10.1021/jm9015747" @default.
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