ArticlePloS one2016
Comparative MD Simulations Indicate a Dual Role for Arg1323.50 in Dopamine-Dependent D2R Activation.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 10 citations in OpenAlex.
- Comparison of the function of two novel human dopamine D2 receptor variants identifies a likely mechanism for their pathogenicity.Biochemical pharmacology · 2024Article
- Allosteric modulation of dopamine DPharmacological reports : PR · 2022Article
- Mechanistic insight into the impact of a bivalent ligand on the structure and dynamics of a GPCR oligomer.Computational and structural biotechnology journal · 2022Article
- Signaling-Biased and Constitutively Active Dopamine D2 Receptor Variant.ACS chemical neuroscience · 2021Article
- Enhancing the Signaling of GPCRs via Orthosteric Ions.ACS central science · 2020Article
- Preferential Coupling of Dopamine DInternational journal of molecular sciences · 2020Article
- Investigating allosteric effects on the functional dynamics of β2-adrenergic ternary complexes with enhanced-sampling simulations.Chemical science · 2017Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
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Abstract
Residue Arg3.50 belongs to the highly conserved DRY-motif of class A GPCRs, which is located at the bottom of TM3. On the one hand, Arg3.50 has been reported to help stabilize the inactive state of GPCRs, but on the other hand has also been shown to be crucial for stabilizing active receptor conformations and mediating receptor-G protein coupling. The combined results of these studies suggest that the exact function of Arg3.50 is likely to be receptor-dependent and must be characterized independently for every GPCR. Consequently, we now present comparative molecular-dynamics simulations that use our recently described inactive-state and Gα-bound active-state homology models of the dopamine D2 receptor (D2R), which are either bound to dopamine or ligand-free, performed to identify the function of Arg1323.50 in D2R. Our results are consistent with a dynamic model of D2R activation in which Arg1323.50 adopts a dual role, both by stabilizing the inactive-state receptor conformation and enhancing dopamine-dependent D2R-G protein coupling.
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