A novel site on the G alpha-protein that recognizes heptahelical receptors

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11120%2F01%3A00003802" target="_blank" >RIV/00216208:11120/01:00003802 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1074/jbc.M004880200" target="_blank" >http://dx.doi.org/10.1074/jbc.M004880200</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1074/jbc.M004880200" target="_blank" >10.1074/jbc.M004880200</a>

Result language
angličtina
Original language name
A novel site on the G alpha-protein that recognizes heptahelical receptors
Original language description
Specific domains of the G-protein a subunit have been shown to control coupling to heptahelical receptors, The extreme N and C termini and a region between alpha4 and alpha5 helices of the G-protein alpha subunit are known to determine selective interaction with the receptors, The metabotropic glutamate receptor 2 activated both mouse G alpha (15) and its human homologue G alpha (16), whereas metabotropic glutamate receptor 8 activated G alpha (15) only. The extreme C-terminal 20 amino acid residues areidentical between the G alpha (15) and G alpha (16) and are therefore unlikely to be involved in coupling selectivity, Our data reveal two regions on G alpha (16) that inhibit its coupling to metabotropic glutamate receptor 8, On a three-dimensional model, both regions are found in a close proximity to the extreme C terminus of G alpha (16). One module comprises alpha4 helix, alpha4-beta6 loop (L9 Loop), beta6 sheet, and alpha5 helix. The other, not described previously, is located with
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Publication year
2001
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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