Crystallization and preliminary X-ray diffraction studies of Drosophila melanogaster Gαo-subunit of heterotrimeric G protein in complex with the RGS domain of CG5036.

Details

Serval ID
serval:BIB_C688AC5098D5
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Crystallization and preliminary X-ray diffraction studies of Drosophila melanogaster Gαo-subunit of heterotrimeric G protein in complex with the RGS domain of CG5036.
Journal
Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Author(s)
Tishchenko S., Gabdulkhakov A., Tin U., Kostareva O., Lin C., Katanaev V.L.
ISSN
1744-3091 (Electronic)
ISSN-L
1744-3091
Publication state
Published
Issued date
2013
Volume
69
Number
Pt 1
Pages
61-64
Language
english
Notes
Publication types: Journal Article
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.
Pubmed
Web of science
Create date
07/02/2013 17:58
Last modification date
20/10/2020 10:08
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