Sandbox Reserved 811: Difference between revisions

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 == Fixation of cations ==
-These domains are along the Na+ and K+ binding sites. Indeed, two sites, which bind 2K+ or 2Na+, locate between helices 4, 5 and 6. The third Na+ is bound on the carboxyl-terminal domain.
+These domains are along the Na+ and <scene name='56/568009/Cation_binding_sites/1'>K+ binding residues</scene>. Indeed, two sites, which bind 2K+ or 2Na+, locate between helices 4, 5 and 6. The third Na+ is bound on the carboxyl-terminal domain.
 It owns a transmembrane domain made of 10 alpha-helix, αM1 to αM10. αM4 and αM6 are partially unwound to form a pocket for K+ ions.
 K+ binding sites, called 1 and 2, are located between αM4, αM5 and αM6.
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 Side chains of Glu 327, Ser 775, Asn 776, Glu 779 and Asp 804 are close enough to the sites to bind the ions, either directly or via a water molecule. Glu 327 possibly controls the extracellular gate of occlusion cavity, it might be controlled by contact with the Leu 97 residue.
-<scene name='56/568009/Cation_binding_sites/1'>K+ binding residues, highlighted in brown</scene>
 Na+ bind at the same sites than K+ ions, which supports the consecutive support model, K+ is being fixed once Na+ released via the same occlusion cavity.The third Na+ binds to a site between the C-terminal domain of theα subunit and several nearby residues.