Sandbox Reserved 1176: Difference between revisions

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====Leu310====

<scene name='72/721548/L310/3'>Leu310</scene> is crucial for interactions with the G alpha subunit through its interactions with Arg167 of the conserved <scene name='72/721548/Dery_motif/1'>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 (Figure 3) and Arg167 interacted with the G alpha subunit leading to the transduction of several different signals involved in leptin signlaing, dopamine regulation, etc. <ref name="SPGP"/> <ref name="Mice"/><ref name="cancer"/><ref name="Schizophrenia"/>

<scene name='72/721548/L310/3'>Leu310</scene> is crucial for interactions with the G alpha subunit through its interactions with Arg167 of 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 (Figure 3) and Arg167 interacted with the G alpha subunit leading to the transduction of several different signals involved in leptin signlaing, dopamine regulation, etc. <ref name="SPGP"/> <ref name="Mice"/><ref name="cancer"/><ref name="Schizophrenia"/>

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Sandbox Reserved 1176: Difference between revisions

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 ====Leu310====
-<scene name='72/721548/L310/3'>Leu310</scene> is crucial for interactions with the G alpha subunit through its interactions with Arg167 of the conserved <scene name='72/721548/Dery_motif/1'>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 (Figure 3) and Arg167 interacted with the G alpha subunit leading to the transduction of several different signals involved in leptin signlaing, dopamine regulation, etc. <ref name="SPGP"/> <ref name="Mice"/><ref name="cancer"/><ref name="Schizophrenia"/>
+<scene name='72/721548/L310/3'>Leu310</scene> is crucial for interactions with the G alpha subunit through its interactions with Arg167 of 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 (Figure 3) and Arg167 interacted with the G alpha subunit leading to the transduction of several different signals involved in leptin signlaing, dopamine regulation, etc. <ref name="SPGP"/> <ref name="Mice"/><ref name="cancer"/><ref name="Schizophrenia"/>
 .