Three-Dimensional Reconstruction of a Full-Size GABAB Receptor
The three-dimensional (3D) pattern of a full-size GABAB receptor has been reconstructed using computer techniques. To simulate a real microenvironment for the GABAB receptor, the latter was embedded in the bilipidic membrane with the corresponding salt-water environment. Since homology modeling o...
Збережено в:
| Дата: | 2015 |
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| Автори: | , , , , , |
| Формат: | Стаття |
| Мова: | English |
| Опубліковано: |
Інститут фізіології ім. О.О. Богомольця НАН України
2015
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| Назва видання: | Нейрофизиология |
| Онлайн доступ: | http://dspace.nbuv.gov.ua/handle/123456789/148215 |
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| Назва журналу: | Digital Library of Periodicals of National Academy of Sciences of Ukraine |
| Цитувати: | Three-Dimensional Reconstruction of a Full-Size GABAB Receptor / A.Yu. Nyporko, A.M. Naumenko, A. Golius, O.V. Tsymbaliuk, L.M. Shapoval, T.L. Davidovska // Нейрофизиология. — 2015. — Т. 47, № 5. — С. 429-440. — Бібліогр.: 45 назв. — англ. |
Репозитарії
Digital Library of Periodicals of National Academy of Sciences of Ukraine| Резюме: | The three-dimensional (3D) pattern of a full-size GABAB receptor has been reconstructed
using computer techniques. To simulate a real microenvironment for the GABAB receptor,
the latter was embedded in the bilipidic membrane with the corresponding salt-water
environment. Since homology modeling of the GABAB receptor is among the computational
methods allowing one to predict 3D coordinates when experimental data are not available, we
reconstructed the structure of a full-size GABAB receptor by stepwise homology modeling of
individual subunit parts. The stability of receptor subunits was evaluated by calculating the
molecular dynamics. It has been found that C-terminal domains of the intracellular receptor
show a tendency toward compaction, and coiled-coil areas form a structure almost identical
to that specified by crystallization of these fragments. The structure obtained can be applied
for further examination of the structural mechanisms of GABAB receptor interaction with
GABA agonists and antagonists. It is quite evident that molecular dynamics computations
might be a valuable tool in probing details of the receptor function. |
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