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

Kód výsledku v 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>

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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

Název v anglickém jazyce

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

Popis výsledku anglicky

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

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

—

Návaznosti

R - Projekt Ramcoveho programu EK

Rok uplatnění

2001

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of Biological Chemistry

ISSN

0021-9258

e-ISSN

—

Svazek periodika

276

Číslo periodika v rámci svazku

5

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

8

Strana od-do

3262-3269

Kód UT WoS článku

000166784900038

EID výsledku v databázi Scopus

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