Testgp: Difference between revisions
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New page: <StructureSection load='3sn6' size='340' side='right' caption='Adrenergic receptor (blue) complex with G protein α subunit (grey), β subunit (green), γ-2 subunit (gold), antibody fragme... |
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The Gαs subunit consists of two domains, the <scene name='70/701430/Alpharas/2'>Ras domain (GαsRas)</scene> and the <scene name='70/701430/Alphahelical/2'>α-helical domain (GαsAH)</scene>. A previous structure of a GTPγS bound (i.e. active, "turned on") Gαs protein (PDB ID: [http://www.rcsb.org/pdb/explore/explore.do?structureId=1AZT 1AZT]) showed that both domains are involved in nucleotide binding, as the nucleotide-binding pocket of the Gαs subunit is formed by the interface between GαsRas and GαsAH<ref>doi:10.1126/science.278.5345.1943</ref>. It was also previously known that the GsαAH domain has a variable position relative to the GsαRas domain between this GTP bound (active) state and the nucleotide free state<ref>DOI:10.1126/science.8266082</ref><ref>doi:10.1073/pnas.1105810108</ref><ref>doi:10.1073/pnas.1113645108</ref><ref>doi:10.1038/nature10488</ref>. However, the β2AR–Gs complex structure of the receptor attached to the empty (no guanosine phosphate attached) G protein enabled comparing it to the active (GTP bound) structure and by that showing <scene name='70/701430/Gamorph/2'>how large this displacement is</scene> - this is probably the most surprising observation arising from the β2AR–Gs complex. | The Gαs subunit consists of two domains, the <scene name='70/701430/Alpharas/2'>Ras domain (GαsRas)</scene> and the <scene name='70/701430/Alphahelical/2'>α-helical domain (GαsAH)</scene>. A previous structure of a GTPγS bound (i.e. active, "turned on") Gαs protein (PDB ID: [http://www.rcsb.org/pdb/explore/explore.do?structureId=1AZT 1AZT]) showed that both domains are involved in nucleotide binding, as the nucleotide-binding pocket of the Gαs subunit is formed by the interface between GαsRas and GαsAH<ref>doi:10.1126/science.278.5345.1943</ref>. It was also previously known that the GsαAH domain has a variable position relative to the GsαRas domain between this GTP bound (active) state and the nucleotide free state<ref>DOI:10.1126/science.8266082</ref><ref>doi:10.1073/pnas.1105810108</ref><ref>doi:10.1073/pnas.1113645108</ref><ref>doi:10.1038/nature10488</ref>. However, the β2AR–Gs complex structure of the receptor attached to the empty (no guanosine phosphate attached) G protein enabled comparing it to the active (GTP bound) structure and by that showing <scene name='70/701430/Gamorph/2'>how large this displacement is</scene> - this is probably the most surprising observation arising from the β2AR–Gs complex. | ||
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