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000817958 1001_ $$0P:(DE-HGF)0$$aVickery, O. N.$$b0
000817958 1112_ $$a60th Annual Meeting of the Biophysical-Society$$cLos Angeles, CA$$d2016-02-27 - 2016-03-02$$wUSA
000817958 245__ $$aInternal sodium in GPCRs strongly responds to transmembrane voltage changes
000817958 260__ $$aCambridge, Mass.$$bCell Press$$c2016
000817958 300__ $$a425a-426a
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000817958 520__ $$aG protein-coupled receptors (GPCRs) are the largest superfamily of membrane proteins in the human genome, mediating the propagation of extracellular ligand binding information into intracellular signal transduction cascades. Crystal structures have revealed a water-filled hydrophilic internal pocket within their transmembrane domain, extending from the orthosteric ligand-binding site to regions near the G protein binding site. Recent high-resolution structures have identified a sodium ion near the base of this pocket, coordinated by highly conserved residues (1,2).
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000817958 7001_ $$0P:(DE-Juel1)156429$$aMachtens, Jan-Philipp$$b1$$ufzj
000817958 7001_ $$0P:(DE-HGF)0$$aTamburrino, G.$$b2
000817958 7001_ $$0P:(DE-HGF)0$$aSeeliger, D.$$b3
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