2003
DOI: 10.1021/ci034069c
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Molecular Dynamics Simulations of the Ligand-Induced Chemical Information Transfer in the 5-HT1AReceptor

Abstract: Comparative molecular dynamics simulations of the 5-HT(1A) receptor in its empty as well as agonist- (i.e. active) and antagonist-bound (i.e. nonactive) forms have been carried out. The agonists 5-HT and (R)-8-OH-DPAT as well as the antagonist WAY100635 have been employed. The results of this study strengthen the hypothesis that the receptor portions close to the E/DRY/W motif, with prominence to the cytosolic extensions of helices 3 and 6, are particularly susceptible to undergo structural modification in res… Show more

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Cited by 26 publications
(92 citation statements)
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“…These interactions are released in the structures of the highly active a 1b -AR mutants, suggesting that both the two anionic amino acids stabilize the inactive state of the receptor. The role of the charge-reinforced H-bond between R3.50 and E6.30 in maintaining the inactive states of GPCRs has been overemphasized by a number of computational and in vitro experiments [23,24,[28][29][30][45][46][47][48][49]. However, the significantly lower conservation of the glutamate/aspartate at position 6.30 (i.e., 32%) compared to the glutamate/aspartate at 3.49 (i.e., 86%) [50] makes its potential role valid only for a very limited number of GPCRs.…”
Section: Single Molecule Computational Modeling Of Gpcrsmentioning
confidence: 99%
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“…These interactions are released in the structures of the highly active a 1b -AR mutants, suggesting that both the two anionic amino acids stabilize the inactive state of the receptor. The role of the charge-reinforced H-bond between R3.50 and E6.30 in maintaining the inactive states of GPCRs has been overemphasized by a number of computational and in vitro experiments [23,24,[28][29][30][45][46][47][48][49]. However, the significantly lower conservation of the glutamate/aspartate at position 6.30 (i.e., 32%) compared to the glutamate/aspartate at 3.49 (i.e., 86%) [50] makes its potential role valid only for a very limited number of GPCRs.…”
Section: Single Molecule Computational Modeling Of Gpcrsmentioning
confidence: 99%
“…Structural features of ligand-induced active and non-active states Over the last 10 years, we have done extensive studies aimed at investigating the propagation of the structural modifications from the ligand binding site to distal receptor domains, following the docking of selected agonists and antagonists into their cognate receptors [31,35,42,43,48,52,53]. Targets of our study have been different members of family A, including a 1b -AR, m3-muscarinic receptor, OTR, 5-HT 1A serotonin receptor, MCHR1, and MCHR2 [31,35,42,43,48,52,53].…”
Section: Single Molecule Computational Modeling Of Gpcrsmentioning
confidence: 99%
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