Sandbox Reserved 969: Difference between revisions
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The lack of selectivity is due to the fact that the NaK channel have an almost identical structure when it is in complex with Na+, K+ or Rb+ : there is no big rearrangement in the structure of the protein depending on the bound ion. So the structure is stable with any ions, so it is non selective. Moreover, it could have a heavy atom contamination but it happens in a smaller extent with K+ than with Na+. | The lack of selectivity is due to the fact that the NaK channel have an almost identical structure when it is in complex with Na+, K+ or Rb+ : there is no big rearrangement in the structure of the protein depending on the bound ion. So the structure is stable with any ions, so it is non selective. Moreover, it could have a heavy atom contamination but it happens in a smaller extent with K+ than with Na+. | ||
The amino-acids of the site 3 participate a lot in the transfert of Na+. In this case, Na+ binds because of an H-bonding interactions between | The amino-acids of the site 3 participate a lot in the transfert of Na+. In this case, Na+ binds because of an H-bonding interactions between <scene name='60/604488/Asp_66/1'>Asp 66</scene> and the backbone amide of Asn68 which stabilize the structure. Furthermore, Val64 and Thr65 form a ion binding cage where Na+ ions tend bind at upper or lower ends (not in the center). | ||
The nature of the ligands are '''carbonyl-carbonyl'''. | The nature of the ligands are '''carbonyl-carbonyl'''. | ||
