Sandbox Reserved 1176: Difference between revisions
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On the extracellular side of the protein is the | On the extracellular side of the protein is the | ||
<scene name='72/721547/Hydrophobic_binding_pocket/5'>hydrophobic binding pocket</scene>. <ref name="SONT"/> | <scene name='72/721547/Hydrophobic_binding_pocket/5'>hydrophobic binding pocket</scene>. <ref name="SONT"/> | ||
One key residue in this pocket is a Phenylalanine at position 358, which takes part in a network of hydrophobic stacking interactions<ref name="SPGP"/>. These interactions stabilize the Trp321 and Tyr324 residues allowing | One key residue in this pocket is a Phenylalanine at position 358, which takes part in a network of hydrophobic stacking interactions<ref name="SPGP"/>. These interactions stabilize the Trp321 and Tyr324 residues allowing to interact with the '''[https://en.wikipedia.org/wiki/C-terminus C-terminal]''' | ||
<scene name='72/721547/ | <scene name='72/721547/Ligand_protein_interactions/8'>Leu13 residue of NTS ligand</scene> | ||
via '''[https://en.wikipedia.org/wiki/Van_der_Waals_force Van der Waals interactions]''' .<ref name="SONT"/><ref name="SPGP"/> | via '''[https://en.wikipedia.org/wiki/Van_der_Waals_force Van der Waals interactions]''' .<ref name="SONT"/><ref name="SPGP"/> | ||
Without the hydrophobic stacking interactions that are facilitated by the Phe358, this binding interaction would be destabilized. Trp321 also participates in these stacking interactions and serves as the boundary between the ligand binding pocket and the Na<sup>+</sup> binding pocket.<ref name="SPGP"/> | Without the hydrophobic stacking interactions that are facilitated by the Phe358, this binding interaction would be destabilized. Trp321 also participates in these stacking interactions and serves as the boundary between the ligand binding pocket and the Na<sup>+</sup> binding pocket.<ref name="SPGP"/> | ||
