Can Specific Protein-Lipid Interactions Stabilize an Active State of the Beta 2 Adrenergic Receptor?. Neale, C., Herce, H., D., Pomès, R., & Garcia, A. Biophys. J., 109(October):1652-1662, 2015.
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Paper doi abstract bibtex
Paper doi abstract bibtex G-protein-coupled receptors are eukaryotic membrane proteins with broad biological and pharmacological rele- vance. Like all membrane-embedded proteins, their location and orientation are influenced by lipids, which can also impact pro- tein function via specific interactions. Extensive simulations totaling 0.25 ms reveal a process in which phospholipids from the membrane’s cytosolic leaflet enter the empty G-protein binding site of an activated b2 adrenergic receptor and form salt-bridge interactions that inhibit ionic lock formation and prolong active-state residency. Simulations of the receptor embedded in an anionic membrane show increased lipid binding, providing a molecular mechanism for the experimental observation that anionic lipids can enhance receptor activity. Conservation of the arginine component of the ionic lock among Rhodopsin-like G-protein- coupled receptors suggests that intracellular lipid ingression between receptor helices H6 and H7 may be a general mechanism for active-state stabilization.
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title = {Can Specific Protein-Lipid Interactions Stabilize an Active State of the Beta 2 Adrenergic Receptor?},
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abstract = {G-protein-coupled receptors are eukaryotic membrane proteins with broad biological and pharmacological rele- vance. Like all membrane-embedded proteins, their location and orientation are influenced by lipids, which can also impact pro- tein function via specific interactions. Extensive simulations totaling 0.25 ms reveal a process in which phospholipids from the membrane’s cytosolic leaflet enter the empty G-protein binding site of an activated b2 adrenergic receptor and form salt-bridge interactions that inhibit ionic lock formation and prolong active-state residency. Simulations of the receptor embedded in an anionic membrane show increased lipid binding, providing a molecular mechanism for the experimental observation that anionic lipids can enhance receptor activity. Conservation of the arginine component of the ionic lock among Rhodopsin-like G-protein- coupled receptors suggests that intracellular lipid ingression between receptor helices H6 and H7 may be a general mechanism for active-state stabilization.},
bibtype = {article},
author = {Neale, Chris and Herce, Henry D and Pomès, Régis and Garcia, Angel},
doi = {10.1016/j.bpj.2015.08.028},
journal = {Biophys. J.},
number = {October}
}Downloads: 0
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