@article{
 title = {Article Can Specific Protein-Lipid Interactions Stabilize an Active State of the Beta},
 type = {article},
 year = {2015},
 identifiers = {[object Object]},
 pages = {1652-1662},
 volume = {109},
 id = {2a916da8-70da-3f70-b74d-f83a06ede1d4},
 created = {2015-10-20T17:27:45.000Z},
 file_attached = {true},
 profile_id = {0633c91d-b6d5-3fcd-9fa3-6021f99f2c58},
 last_modified = {2015-10-20T17:28:14.000Z},
 read = {false},
 starred = {false},
 authored = {true},
 confirmed = {true},
 hidden = {false},
 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},
 journal = {Biophys. J.},
 number = {October}
}

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