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- W2026357130 abstract "Abstract: A possible molecular mechanism for the constitutive activity of mutants of the angiotensin type 1 receptor (AT 1 ) at position 111 was suggested by molecular modeling. This involves a cascade of conformational changes in spatial positions of side chains along transmembrane helix (TM3) from L112 to Y113 to F117, which in turn, results in conformational changes in TM4 (residues I152 and M155) leading to the movement of TM4 as a whole. The mechanism is consistent with the available data of site‐directed mutagenesis, as well as with correct predictions of constitutive activity of mutants L112F and L112C. It was also predicted that the double mutant N111G/L112A might possess basal constitutive activity comparable with that of the N111G mutant, whereas the double mutants N111G/Y113A, N111G/F117A, and N111G/I152A would have lower levels of basal activity. Experimental studies of the above double mutants showed significant constitutive activity of N111G/L112A and N111G/F117A. The basal activity of N111G/I152A was higher than expected, and that of N111G/Y113A was not determined due to poor expression of the mutant. The proposed mechanism of constitutive activity of the AT 1 receptor reveals a novel nonsimplistic view on the general problem of constitutive activity, and clearly demonstrates the inherent complexity of the process of G protein‐coupled receptor (GPCR) activation." @default.
- W2026357130 created "2016-06-24" @default.
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- W2026357130 date "2005-11-01" @default.
- W2026357130 modified "2023-10-15" @default.
- W2026357130 title "Molecular mechanisms of constitutive activity: mutations at position 111 of the angiotensin AT1 receptor" @default.
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- W2026357130 doi "https://doi.org/10.1111/j.1399-3011.2005.00293.x" @default.
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