Beta2 adrenergic receptor-Gs protein complex: Difference between revisions
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== G-Protein-GPCR Intercations == | == G-Protein-GPCR Intercations == | ||
The a5-helix of Gas 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 | The a5-helix of Gas 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 a5-helix against Arg 131 of the conserved DRY sequence inTM3. Arg 131 also packs against Tyr 326 of the conserved NPxxY sequence in TM7</scene>. As the a5-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 b2AR 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 b2AR. | ||
NPxxY sequence in TM7</scene> | |||
== G-Protein Cycle == | == G-Protein Cycle == | ||
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The Gαs subunit consists of two domains, the Ras domain (αRas) and the α-helical domain (αAH). Both are involved in nucleotide binding. In the nucleotide-free state, the αAH domain has a variable position relative the αRas domain. | The Gαs subunit consists of two domains, the Ras domain (αRas) and the α-helical domain (αAH). Both are involved in nucleotide binding. In the nucleotide-free state, the αAH domain has a variable position relative the αRas domain. | ||
==See Also== | ==See Also== | ||
*[[Adrenergic receptor|Adrenergic receptor]] | *[[Adrenergic receptor|Adrenergic receptor]] | ||