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
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