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<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]'''

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 <scene name='72/721547/Ligand_protein_interactions/8'>Tyr324</scene> to interact with the '''[https://en.wikipedia.org/wiki/C-terminus C-terminal]'''

<scene name='72/721547/Hydrophobic_binding_pocket/6'>Leu13 residue of the NTS ligand</scene>

via '''[https://en.wikipedia.org/wiki/Van_der_Waals_force Van der Waals interactions]''' .<ref name="SONT"/><ref name="SPGP"/>

Line 32:

====Leu310====

~~<scene name='72/721547/Ligand_protein_interactions/8'>Leu310</scene>~~ is crucial for interactions with the G alpha subunit by positioning Arg167 in the conserved <scene name='72/721548/Dery_motif/2'>D/ERY motif</scene><ref name="SPGP"/>. When Leu310 was substituted with alanine, Arg167 was able to form a stabilizing hydrogen bonding network with Asn257, Ser164 and Gly306, which oriented Arg167 in a position that was unfavorable for contacting the G alpha subunit. When residue 310 was converted back to leucine, this hydrogen bonding network was sterically unfavorable and Arg167 interacted with the G alpha subunit<ref name="SPGP"/> leading to the transduction of several different signals involved in dopamine regulation<ref name="Schizophrenia"/>, leptin signlaing<ref name="Mice"/>, and tumor growth<ref name="cancer"/>.

is crucial for interactions with the G alpha subunit by positioning Arg167 in the conserved <scene name='72/721548/Dery_motif/2'>D/ERY motif</scene><ref name="SPGP"/>. When Leu310 was substituted with alanine, Arg167 was able to form a stabilizing hydrogen bonding network with Asn257, Ser164 and Gly306, which oriented Arg167 in a position that was unfavorable for contacting the G alpha subunit. When residue 310 was converted back to leucine, this hydrogen bonding network was sterically unfavorable and Arg167 interacted with the G alpha subunit<ref name="SPGP"/> leading to the transduction of several different signals involved in dopamine regulation<ref name="Schizophrenia"/>, leptin signlaing<ref name="Mice"/>, and tumor growth<ref name="cancer"/>.

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Sandbox Reserved 1176: Difference between revisions

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@@ 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<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]'''
+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 <scene name='72/721547/Ligand_protein_interactions/8'>Tyr324</scene> to interact with the '''[https://en.wikipedia.org/wiki/C-terminus C-terminal]'''
 <scene name='72/721547/Hydrophobic_binding_pocket/6'>Leu13 residue of the NTS ligand</scene>
 via '''[https://en.wikipedia.org/wiki/Van_der_Waals_force Van der Waals interactions]''' .<ref name="SONT"/><ref name="SPGP"/>
@@ Line 32: / Line 32: @@
 ====Leu310====
-<scene name='72/721547/Ligand_protein_interactions/8'>Leu310</scene> is crucial for interactions with the G alpha subunit by positioning Arg167 in the conserved <scene name='72/721548/Dery_motif/2'>D/ERY motif</scene><ref name="SPGP"/>. When Leu310 was substituted with alanine, Arg167 was able to form a stabilizing hydrogen bonding network with  Asn257, Ser164 and Gly306, which oriented Arg167 in a position that was unfavorable for contacting the G alpha subunit. When residue 310 was converted back to leucine, this hydrogen bonding network was sterically unfavorable and Arg167 interacted with the G alpha subunit<ref name="SPGP"/>  leading to the transduction of several different signals involved in dopamine regulation<ref name="Schizophrenia"/>, leptin signlaing<ref name="Mice"/>, and tumor growth<ref name="cancer"/>.
+ is crucial for interactions with the G alpha subunit by positioning Arg167 in the conserved <scene name='72/721548/Dery_motif/2'>D/ERY motif</scene><ref name="SPGP"/>. When Leu310 was substituted with alanine, Arg167 was able to form a stabilizing hydrogen bonding network with  Asn257, Ser164 and Gly306, which oriented Arg167 in a position that was unfavorable for contacting the G alpha subunit. When residue 310 was converted back to leucine, this hydrogen bonding network was sterically unfavorable and Arg167 interacted with the G alpha subunit<ref name="SPGP"/>  leading to the transduction of several different signals involved in dopamine regulation<ref name="Schizophrenia"/>, leptin signlaing<ref name="Mice"/>, and tumor growth<ref name="cancer"/>.
 .