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Exploration of N-arylpiperazine Binding Sites of D2 Dopaminergic Receptor

Нема приказа
Аутори
Šoškić, Vukić
Šukalović, Vladimir
Kostić Rajačić, Slađana
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документу
Апстракт
The crystal structures of the D3 dopamine receptor and several other G-protein coupled receptors (GPCRs) were published in recent times. Those 3D structures are used by us and other scientists as a template for the homology modeling and ligand docking analysis of related GPCRs. Our main scientific interest lies in the field of pharmacologically active N-arylpiperazines that exhibit antipsychotic and/or antidepressant properties, and as such are dopaminergic and serotonergic receptor ligands. In this short review article we are presenting synthesis and biological data on the new N-arylpipereazine as well our results on molecular modeling of the interactions of those N-arylpiperazines with the model of D2 dopamine receptors. To obtain that model the crystal structure of the D3 dopamine receptor was used. Our results show that the N-arylpiperazines binding site consists of two pockets: one is the orthosteric binding site where the N-arylpiperazine part of the ligand is docked and the seco...nd is a non-canonical accessory binding site for N-arylpipereazine that is formed by a second extracellular loop (ecl2) of the receptor. Until now, the structure of this receptor region was unresolved in crystal structure analyses of the D3 dopamine receptor. To get a more complete picture of the ligand - receptor interaction, DFT quantum mechanical calculations on N-arylpiperazine were performed and the obtained models were used to examine those interactions.

Кључне речи:
Dopamine D2 receptor / G-protein coupled receptors / molecular modelling / N-arylpiperazines
Извор:
Mini-Reviews in Medicinal Chemistry, 2015, 15, 12, 988-1001
Издавач:
  • Bentham Science Publ Ltd, Sharjah
Финансирање / пројекти:
  • Проучавање односа структуре и активности новосинтетисаних биолошки активних супстанци (RS-172032)

DOI: 10.2174/138955751512150731112448

ISSN: 1389-5575

PubMed: 25723457

WoS: 000358803500005

Scopus: 2-s2.0-84939832374
[ Google Scholar ]
9
10
URI
https://cer.ihtm.bg.ac.rs/handle/123456789/1619
Колекције
  • Radovi istraživača / Researchers' publications
Институција/група
IHTM
TY  - JOUR
AU  - Šoškić, Vukić
AU  - Šukalović, Vladimir
AU  - Kostić Rajačić, Slađana
PY  - 2015
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1619
AB  - The crystal structures of the D3 dopamine receptor and several other G-protein coupled receptors (GPCRs) were published in recent times. Those 3D structures are used by us and other scientists as a template for the homology modeling and ligand docking analysis of related GPCRs. Our main scientific interest lies in the field of pharmacologically active N-arylpiperazines that exhibit antipsychotic and/or antidepressant properties, and as such are dopaminergic and serotonergic receptor ligands. In this short review article we are presenting synthesis and biological data on the new N-arylpipereazine as well our results on molecular modeling of the interactions of those N-arylpiperazines with the model of D2 dopamine receptors. To obtain that model the crystal structure of the D3 dopamine receptor was used. Our results show that the N-arylpiperazines binding site consists of two pockets: one is the orthosteric binding site where the N-arylpiperazine part of the ligand is docked and the second is a non-canonical accessory binding site for N-arylpipereazine that is formed by a second extracellular loop (ecl2) of the receptor. Until now, the structure of this receptor region was unresolved in crystal structure analyses of the D3 dopamine receptor. To get a more complete picture of the ligand - receptor interaction, DFT quantum mechanical calculations on N-arylpiperazine were performed and the obtained models were used to examine those interactions.
PB  - Bentham Science Publ Ltd, Sharjah
T2  - Mini-Reviews in Medicinal Chemistry
T1  - Exploration of N-arylpiperazine Binding Sites of D2 Dopaminergic Receptor
VL  - 15
IS  - 12
SP  - 988
EP  - 1001
DO  - 10.2174/138955751512150731112448
ER  - 
@article{
author = "Šoškić, Vukić and Šukalović, Vladimir and Kostić Rajačić, Slađana",
year = "2015",
abstract = "The crystal structures of the D3 dopamine receptor and several other G-protein coupled receptors (GPCRs) were published in recent times. Those 3D structures are used by us and other scientists as a template for the homology modeling and ligand docking analysis of related GPCRs. Our main scientific interest lies in the field of pharmacologically active N-arylpiperazines that exhibit antipsychotic and/or antidepressant properties, and as such are dopaminergic and serotonergic receptor ligands. In this short review article we are presenting synthesis and biological data on the new N-arylpipereazine as well our results on molecular modeling of the interactions of those N-arylpiperazines with the model of D2 dopamine receptors. To obtain that model the crystal structure of the D3 dopamine receptor was used. Our results show that the N-arylpiperazines binding site consists of two pockets: one is the orthosteric binding site where the N-arylpiperazine part of the ligand is docked and the second is a non-canonical accessory binding site for N-arylpipereazine that is formed by a second extracellular loop (ecl2) of the receptor. Until now, the structure of this receptor region was unresolved in crystal structure analyses of the D3 dopamine receptor. To get a more complete picture of the ligand - receptor interaction, DFT quantum mechanical calculations on N-arylpiperazine were performed and the obtained models were used to examine those interactions.",
publisher = "Bentham Science Publ Ltd, Sharjah",
journal = "Mini-Reviews in Medicinal Chemistry",
title = "Exploration of N-arylpiperazine Binding Sites of D2 Dopaminergic Receptor",
volume = "15",
number = "12",
pages = "988-1001",
doi = "10.2174/138955751512150731112448"
}
Šoškić, V., Šukalović, V.,& Kostić Rajačić, S.. (2015). Exploration of N-arylpiperazine Binding Sites of D2 Dopaminergic Receptor. in Mini-Reviews in Medicinal Chemistry
Bentham Science Publ Ltd, Sharjah., 15(12), 988-1001.
https://doi.org/10.2174/138955751512150731112448
Šoškić V, Šukalović V, Kostić Rajačić S. Exploration of N-arylpiperazine Binding Sites of D2 Dopaminergic Receptor. in Mini-Reviews in Medicinal Chemistry. 2015;15(12):988-1001.
doi:10.2174/138955751512150731112448 .
Šoškić, Vukić, Šukalović, Vladimir, Kostić Rajačić, Slađana, "Exploration of N-arylpiperazine Binding Sites of D2 Dopaminergic Receptor" in Mini-Reviews in Medicinal Chemistry, 15, no. 12 (2015):988-1001,
https://doi.org/10.2174/138955751512150731112448 . .

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