首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Crystallization and preliminary X-ray diffraction studies of Drosophila melanogaster G alpha o-subunit of heterotrimeric G protein in complex with the RGS domain of CG5036
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Crystallization and preliminary X-ray diffraction studies of Drosophila melanogaster G alpha o-subunit of heterotrimeric G protein in complex with the RGS domain of CG5036

机译:与CG5036的RGS结构域复合的异三聚体G蛋白的果蝇果蝇G alpha o-亚基的结晶和初步X射线衍射研究

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摘要

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 G alpha-subunits. Although omnipresent in eukaryotes, RGS proteins have not been adequately analysed in non-mammalian organisms. The Drosophila melanogaster G alpha o-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 angstrom resolution using a synchrotron-radiation source.
机译:G蛋白信号转导(RGS)蛋白的调节剂通过其保守的RGS域负调控异源三聚体G蛋白信号转导。 RGS结构域充当GTPase激活蛋白,可加快Gα亚基激活形式的GTP水解速度。尽管真核生物中普遍存在RGS蛋白,但尚未在非哺乳动物生物中对其进行充分的分析。果蝇果蝇Gαo亚基和它的相互作用伙伴CG5036的RGS结构域已经过生产和纯化。报道了使用PEG 4000作为结晶剂对两种蛋白质的复合物进行结晶和初步X射线晶体学分析的报道。使用同步辐射源将衍射数据收集到2.0埃分辨率。

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