Sandbox Reserved 1176: Difference between revisions

Line 10:

On the extracellular side of the protein is the

<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. These interactions stabilize the Trp321 and Tyr324 residues allowing Tyr324 to interact with the '''[https://en.wikipedia.org/wiki/C-terminus C-terminal]'''

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 Tyr324 to interact with the '''[https://en.wikipedia.org/wiki/C-terminus C-terminal]'''

<scene name='72/721547/Ligand_protein_interactions/7'>Leu13 residue of the NTS ligand</scene>

via '''[https://en.wikipedia.org/wiki/Van_der_Waals_force Van der Waals interactions]''' .

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 sodium binding pocket.

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 sodium binding pocket. <ref name="SPGP"/>

===Na<sup>+</sup> Binding Pocket===

Sandbox Reserved 1176: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 10: / Line 10: @@
 On the extracellular side of the protein is the
 <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. These interactions stabilize the Trp321 and Tyr324 residues allowing Tyr324 to interact with the '''[https://en.wikipedia.org/wiki/C-terminus C-terminal]'''
+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 Tyr324 to interact with the '''[https://en.wikipedia.org/wiki/C-terminus C-terminal]'''
 <scene name='72/721547/Ligand_protein_interactions/7'>Leu13 residue of the NTS ligand</scene>
-via '''[https://en.wikipedia.org/wiki/Van_der_Waals_force Van der Waals interactions]''' .
+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 sodium binding pocket.
+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 sodium binding pocket. <ref name="SPGP"/>
 ===Na<sup>+</sup> Binding Pocket===