ArticleBiophysical journal2016
Ultraslow Water-Mediated Transmembrane Interactions Regulate the Activation of A2A Adenosine Receptor.
Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 40 citations in OpenAlex.
- Ligand-Induced Biased Activation of GPCRs: Recent Advances and New Directions from In Silico Approaches.Molecules (Basel, Switzerland) · 2025Review
- Descriptive molecular pharmacology of the δ opioid receptor (DOR): A computational study with structural approach.PloS one · 2024Article
- Global insights into the fine tuning of human ACell reports · 2022Article
- Mechanistic basis of GPCR activation explored by ensemble refinement of crystallographic structures.Protein science : a publication of the Protein Society · 2022Article
- A Statistical Journey through the Topological Determinants of the β2 Adrenergic Receptor Dynamics.Entropy (Basel, Switzerland) · 2022Article
- The origin and impact of bound water around intrinsically disordered proteins.Biophysical journal · 2022Article
- Implications for human odor sensing revealed from the statistics of odorant-receptor interactions.PLoS computational biology · 2018Article
- Signaling within Allosteric Machines: Signal Transmission Pathways Inside G Protein-Coupled Receptors.Molecules (Basel, Switzerland) · 2017Review
- Gorge Motions of Acetylcholinesterase Revealed by Microsecond Molecular Dynamics Simulations.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Water molecules inside a G-protein coupled receptor (GPCR) have recently been spotlighted in a series of crystal structures. To decipher the dynamics and functional roles of internal water molecules in GPCR activity, we studied the A2A adenosine receptor using microsecond molecular-dynamics simulations. Our study finds that the amount of water flux across the transmembrane (TM) domain varies depending on the receptor state, and that the water molecules of the TM channel in the active state flow three times more slowly than those in the inactive state. Depending on the location in solvent-protein interface as well as the receptor state, the average residence time of water in each residue varies from ∼O(10(2)) ps to ∼O(10(2)) ns. Especially, water molecules, exhibiting ultraslow relaxation (∼O(10(2)) ns) in the active state, are found around the microswitch residues that are considered activity hotspots for GPCR function. A continuous allosteric network spanning the TM domain, arising from water-mediated contacts, is unique in the active state, underscoring the importance of slow water molecules in the activation of GPCRs.
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