Beta2 adrenergic receptor-Gs protein complex: Difference between revisions
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The α5-helix of Gαs docks into a cavity formed on the intracellular side of the receptor by the opening of transmembrane helices 5 and 6. Within the transmembrane core, the interactions are primarily non-polar - an exception involves <scene name='70/701430/Receptor_g_protein_interaction/4'>packing of Tyr 391 of the α5-helix against Arg 131 of the conserved DRY sequence in TM3. Arg 131 also packs against Tyr 326 of the conserved NPxxY sequence in TM7</scene>. As the α5-helix exits the receptor it forms a network of polar interactions with TM5 and TM3. Receptor residues <scene name='70/701430/Receptor_gprotein_interaction2/1'>Thr 68 and Asp 130 interact with the ICL2 helix of the β2AR via Tyr 141, positioning the helix so that Phe 139 of the receptor docks into a hydrophobic pocket on the G protein surface</scene>, thereby structurally linking receptor–G protein interactions with the highly conserved DRY motif of the β2AR. | The α5-helix of Gαs docks into a cavity formed on the intracellular side of the receptor by the opening of transmembrane helices 5 and 6. Within the transmembrane core, the interactions are primarily non-polar - an exception involves <scene name='70/701430/Receptor_g_protein_interaction/4'>packing of Tyr 391 of the α5-helix against Arg 131 of the conserved DRY sequence in TM3. Arg 131 also packs against Tyr 326 of the conserved NPxxY sequence in TM7</scene>. As the α5-helix exits the receptor it forms a network of polar interactions with TM5 and TM3. Receptor residues <scene name='70/701430/Receptor_gprotein_interaction2/1'>Thr 68 and Asp 130 interact with the ICL2 helix of the β2AR via Tyr 141, positioning the helix so that Phe 139 of the receptor docks into a hydrophobic pocket on the G protein surface</scene>, thereby structurally linking receptor–G protein interactions with the highly conserved DRY motif of the β2AR. | ||
== G-Protein Cycle == | == G-Protein Activation Cycle == | ||
[[Image:ImgSmall1.jpg|500px|G protein cycle for the β2AR–Gs complex. Reprinted by permission from Macmillan Publishers Ltd on behalf of Cancer Research UK: Nature 477, 549–555, copyright 2011]] | [[Image:ImgSmall1.jpg|500px|G protein cycle for the β2AR–Gs complex. Reprinted by permission from Macmillan Publishers Ltd on behalf of Cancer Research UK: Nature 477, 549–555, copyright 2011]] | ||