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Allosteric sodium in class A GPCR signaling

www.cell.com/trends/biochemical-sciences/fulltext/S0968-0004(14)00048-6

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  • the Na+ and water pocket collapses in size from ∼200 to <70 Å3 due to the activation-related movements of the TM helices.

  • Conformational analysis and molecular dynamics studies for A2AAR suggest that such a collapsed pocket in the active-like states of GPCRs is incompatible with Na+ binding [30].

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