Sandbox Reserved 1176: Difference between revisions

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====Glu166====

Although the role of <scene name='72/721548/E166/3'>Glu166</scene> in G-protein activity is not quite as clear as it is for <scene name='72/721548/L310/3'>Leu310</scene> or <scene name='72/721547/Hydrophobic_binding_pocket/5'>Phe358</scene>, substituting this residue for an alanine significantly reduced '''[https://en.wikipedia.org/wiki/Active_site catalytic]''' nucleotide exchange <ref name="SPGP"/>. Glu166 is part of a D/ERY motif that is highly conserved in class A GPCRs and includes Arg167 and Tyr168. To determine a role for Glu166, other class A GPCRs were structurally analyzed. Researchers <ref name="SPGP"/> hypothesize that E166 in NTSR1 interacts with Val102, Thr101,and weakly interacts with His105 to stabilize the G protein. Researchers <ref name="SPGP"/> have also noted the possibility of an important connection between the D/ERY motif and intracellular loop 2, which plays a role in the dissociation of the receptor-G protein complex with GTP present. M181 is believed to link the D/ERY motif and ICL2. <ref name="SPGP"/>

Although the role of <scene name='72/721548/E166/4'>Glu166</scene> in G-protein activity is not quite as clear as it is for <scene name='72/721548/L310/3'>Leu310</scene> or <scene name='72/721547/Hydrophobic_binding_pocket/5'>Phe358</scene>, substituting this residue for an alanine significantly reduced '''[https://en.wikipedia.org/wiki/Active_site catalytic]''' nucleotide exchange <ref name="SPGP"/>. Glu166 is part of a D/ERY motif that is highly conserved in class A GPCRs and includes Arg167 and Tyr168. To determine a role for Glu166, other class A GPCRs were structurally analyzed. Researchers <ref name="SPGP"/> hypothesize that E166 in NTSR1 interacts with Val102, Thr101,and weakly interacts with His105 to stabilize the G protein. Researchers <ref name="SPGP"/> have also noted the possibility of an important connection between the D/ERY motif and intracellular loop 2, which plays a role in the dissociation of the receptor-G protein complex with GTP present. M181 is believed to link the D/ERY motif and ICL2. <ref name="SPGP"/>

Sandbox Reserved 1176: Difference between revisions

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Revision as of 01:26, 22 April 2016 view source Danny Cotter (talk \| contribs) 188 edits No edit summary ← Older edit		Revision as of 01:30, 22 April 2016 view source Danny Cotter (talk \| contribs) 188 edits No edit summary Newer edit →
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	====Glu166====		====Glu166====

	Although the role of <scene name='72/721548/E166/3'>Glu166</scene> in G-protein activity is not quite as clear as it is for <scene name='72/721548/L310/3'>Leu310</scene> or <scene name='72/721547/Hydrophobic_binding_pocket/5'>Phe358</scene>, substituting this residue for an alanine significantly reduced '''[https://en.wikipedia.org/wiki/Active_site catalytic]''' nucleotide exchange <ref name="SPGP"/>. Glu166 is part of a D/ERY motif that is highly conserved in class A GPCRs and includes Arg167 and Tyr168. To determine a role for Glu166, other class A GPCRs were structurally analyzed. Researchers <ref name="SPGP"/> hypothesize that E166 in NTSR1 interacts with Val102, Thr101,and weakly interacts with His105 to stabilize the G protein. Researchers <ref name="SPGP"/> have also noted the possibility of an important connection between the D/ERY motif and intracellular loop 2, which plays a role in the dissociation of the receptor-G protein complex with GTP present. M181 is believed to link the D/ERY motif and ICL2. <ref name="SPGP"/>		Although the role of <scene name='72/721548/E166/4'>Glu166</scene> in G-protein activity is not quite as clear as it is for <scene name='72/721548/L310/3'>Leu310</scene> or <scene name='72/721547/Hydrophobic_binding_pocket/5'>Phe358</scene>, substituting this residue for an alanine significantly reduced '''[https://en.wikipedia.org/wiki/Active_site catalytic]''' nucleotide exchange <ref name="SPGP"/>. Glu166 is part of a D/ERY motif that is highly conserved in class A GPCRs and includes Arg167 and Tyr168. To determine a role for Glu166, other class A GPCRs were structurally analyzed. Researchers <ref name="SPGP"/> hypothesize that E166 in NTSR1 interacts with Val102, Thr101,and weakly interacts with His105 to stabilize the G protein. Researchers <ref name="SPGP"/> have also noted the possibility of an important connection between the D/ERY motif and intracellular loop 2, which plays a role in the dissociation of the receptor-G protein complex with GTP present. M181 is believed to link the D/ERY motif and ICL2. <ref name="SPGP"/>