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While the molecular structures of angiotensin II (Ang II) type 1 (AT 1 ) receptor blockers (ARBs) are very similar, they are also slightly different. Although each ARB has been shown to exhibit a unique mode of binding to AT 1  receptor, different positions of the AT 1  receptor have been analyzed and computational modeling has been performed using different crystal structures for the receptor as a template and different kinds of software. Therefore, we systematically analyzed the critical positions of the AT 1  receptor, Tyr 113 , Tyr 184 , Lys 199 , His 256  and Gln 257  using a mutagenesis study, and subsequently performed computational modeling of the binding of ARBs to AT 1  receptor using CXCR4 receptor as a new template and a single version of software. The interactions between Tyr 113  in the AT 1  receptor and the hydroxyl group of olmesartan, between Lys 199  and carboxyl or tetrazole groups, and between His 256  or Gln 257  and the tetrazole group were studied. The common structure, a tetrazole group, of most ARBs similarly bind to Lys 199 , His 256  and Gln 257  of AT 1  receptor. Lys 199  in the AT 1  receptor binds to the carboxyl group of EXP3174, candesartan and azilsartan, whereas oxygen in the amidecarbonyl group of valsartan may bind to Lys 199 . The benzimidazole portion of telmisartan may bind to a lipophilic pocket that includes Tyr 113 . On the other hand, the n-butyl group of irbesartan may bind to Tyr 113 . In conclusion, we confirmed that the slightly different structures of ARBs may be critical for binding to AT 1  receptor and for the formation of unique modes of binding.

Reassessment of the Unique Mode of Binding between Angiotensin II Type 1 Receptor and Their Blockers