Mapping the agonist-binding site of GABAB type 1 subunit sheds light on the activation process of GABAB receptors
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11120%2F00%3A00003720" target="_blank" >RIV/00216208:11120/00:00003720 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1074/jbc.M007848200" target="_blank" >http://dx.doi.org/10.1074/jbc.M007848200</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1074/jbc.M007848200" target="_blank" >10.1074/jbc.M007848200</a>
Alternative languages
Result language
angličtina
Original language name
Mapping the agonist-binding site of GABAB type 1 subunit sheds light on the activation process of GABAB receptors
Original language description
The gamma -amino-n-butyric acid type B (GABA(B)) receptor is composed of two subunits, GABA(B)1 and GABA(B)2, belonging to the family 3 heptahelix receptors. These proteins possess two domains, a seven transmembrane core and an extracellular domain containing the agonist binding site. This binding domain is likely to fold like bacterial periplasmic binding proteins that are constituted of two lobes that close upon ligand binding. Here, using molecular modeling and site-directed mutagenesis, we have identified residues in the GABA(B)1 subunit that are critical for agonist binding and activation of the heteromeric receptor. Our data suggest that two residues (Ser(246) and Asp(471)) located within lobe I form H bonds and a salt bridge with carboxylic andamino groups of GABA, respectively, demonstrating the pivotal role of lobe I in agonist binding. Interestingly, our data also suggest that a residue within lobe II (Tyr(366)) interacts with the agonists in a closed form model of the bindi
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
FD - Oncology and haematology
OECD FORD branch
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Result continuities
Project
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Continuities
S - Specificky vyzkum na vysokych skolach
Others
Publication year
2000
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of Biological Chemistry
ISSN
0021-9258
e-ISSN
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Volume of the periodical
275
Issue of the periodical within the volume
52
Country of publishing house
US - UNITED STATES
Number of pages
9
Pages from-to
41166-41174
UT code for WoS article
000166114600069
EID of the result in the Scopus database
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