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- W2020138204 abstract "Regulator of G-protein signalling (RGS) proteins negatively regulate heterotrimeric G-protein signalling through their conserved RGS domains. RGS domains act as GTPase-activating proteins, accelerating the GTP hydrolysis rate of the activated form of Gα-subunits. Although omnipresent in eukaryotes, RGS proteins have not been adequately analysed in non-mammalian organisms. The Drosophila melanogaster Gαo-subunit and the RGS domain of its interacting partner CG5036 have been overproduced and purified; the crystallization of the complex of the two proteins using PEG 4000 as a crystallizing agent and preliminary X-ray crystallographic analysis are reported. Diffraction data were collected to 2.0 Å resolution using a synchrotron-radiation source." @default.
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- W2020138204 date "2012-12-20" @default.
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- W2020138204 title "Crystallization and preliminary X-ray diffraction studies of<i>Drosophila melanogaster</i>Gαo-subunit of heterotrimeric G protein in complex with the RGS domain of CG5036" @default.
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- W2020138204 doi "https://doi.org/10.1107/s174430911204804x" @default.
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