Beta2 adrenergic receptor-Gs protein complex: Difference between revisions
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The figure shows the G Protein cycle <ref>doi:10.1038/nature10361</ref> - an extracellular agonist binds to the β2AR leads <scene name='70/701430/Receptor_morphing_animation/2'>to conformational rearrangements of the cytoplasmic ends of transmembrane segments</scene> that enable the Gs heterotrimer to bind the receptor. GDP is released from the α subunit upon formation of β2AR–Gs complex. The GTP binds to the nucleotide-free α subunit resulting in dissociation of the α and βγ subunits from the receptor. The subunits regulate their respective effector proteins adenylyl cyclase (AC) and Ca2+ channels. The Gs heterotrimer reassembles from α and βγ subunits following hydrolysis of GTP to GDP in the α subunit. | The figure shows the G Protein cycle <ref>doi:10.1038/nature10361</ref> - an extracellular agonist binds to the β2AR leads <scene name='70/701430/Receptor_morphing_animation/2'>to conformational rearrangements of the cytoplasmic ends of transmembrane segments</scene> that enable the Gs heterotrimer to bind the receptor. GDP is released from the α subunit upon formation of β2AR–Gs complex. The GTP binds to the nucleotide-free α subunit resulting in dissociation of the α and βγ subunits from the receptor. The subunits regulate their respective effector proteins adenylyl cyclase (AC) and Ca2+ channels. The Gs heterotrimer reassembles from α and βγ subunits following hydrolysis of GTP to GDP in the α subunit. | ||
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<scene name='70/701430/Gamorph/1'> | == G-Protein variability == | ||
The Gαs subunit consists of two domains, the Ras domain (αRas) and the α-helical domain (αAH). Both are involved in nucleotide binding. A big discovery made thanks to this structure is that the G alpha subunit has large variability between its GTP bound (active) and nucleotide free states, where <scene name='70/701430/Gamorph/1'>the αAH domain has a variable position relative to the αRas domain</scene> | |||
==See Also== | ==See Also== |