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Chien, Ellen Y.T; Liu, Wei; Zhao, Qiang; Katritch, Vsevolod; Won Han, Gye; Hanson, Michael A; Shi, Lei; Newman, Amy Hauck; Javitch, Jonathan A; Cherezov, Vadim; Stevens, Raymond C
Science (American Association for the Advancement of Science), 11/2010, Letnik: 330, Številka: 6007Journal Article
Dopamine modulates movement, cognition, and emotion through activation of dopamine G protein-coupled receptors in the brain. The crystal structure of the human dopamine D3 receptor (D3R) in complex with the small molecule D2R/D3R-specific antagonist eticlopride reveals important features of the ligand binding pocket and extracellular loops. On the intracellular side of the receptor, a locked conformation of the ionic lock and two distinctly different conformations of intracellular loop 2 are observed. Docking of R-22, a D3R-selective antagonist, reveals an extracellular extension of the eticlopride binding site that comprises a second binding pocket for the aryl amide of R-22, which differs between the highly homologous D2R and D3R. This difference provides direction to the design of D3R-selective agents for treating drug abuse and other neuropsychiatric indications.
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in: SICRIS
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