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6c38
From Proteopedia
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/DRD2_HUMAN DRD2_HUMAN]] Dopamine receptor whose activity is mediated by G proteins which inhibit adenylyl cyclase (By similarity).<ref>PMID:21645528</ref> <ref>PMID:17264214</ref> | [[http://www.uniprot.org/uniprot/DRD2_HUMAN DRD2_HUMAN]] Dopamine receptor whose activity is mediated by G proteins which inhibit adenylyl cyclase (By similarity).<ref>PMID:21645528</ref> <ref>PMID:17264214</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Dopamine is a neurotransmitter that has been implicated in processes as diverse as reward, addiction, control of coordinated movement, metabolism and hormonal secretion. Correspondingly, dysregulation of the dopaminergic system has been implicated in diseases such as schizophrenia, Parkinson's disease, depression, attention deficit hyperactivity disorder, nausea and vomiting, among others. Dopamine's actions are mediated by a family of five G-protein coupled receptors (GPCRs) (viz. D1, D2, D3, D4 and D5)(1). The D2 dopamine receptor (DRD2) is the primary target for both typical(2) and atypical(3,4) antipsychotic drugs, and for Parkinson's disease drugs. Unfortunately, many drugs targeting DRD2 frequently cause serious and potentially life-threatening side effects due to promiscuous activities against related receptors(4,5). Accordingly, a molecular understanding of DRD2 structure and function could provide a template for the design of safer and more effective medications. Here we provide the crystal structure of DRD2 in complex with the widely prescribed atypical antipsychotic drug risperidone. The DRD2-risperidone structure reveals an unexpected mode of antipsychotic drug binding to dopamine receptors, and illuminates structural determinants essential for the actions of risperidone and related drugs at DRD2. | ||
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| + | Structure of the D2 dopamine receptor bound to the atypical antipsychotic drug risperidone.,Wang S, Che T, Levit A, Shoichet BK, Wacker D, Roth BL Nature. 2018 Jan 24. pii: nature25758. doi: 10.1038/nature25758. PMID:29466326<ref>PMID:29466326</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6c38" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 06:22, 8 March 2018
Structure of the D2 Dopamine Receptor Bound to the Atypical Antipsychotic Drug Risperidone
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Categories: Human | Lysozyme | Che, T | Levit, A | Roth, B L | Shoichet, B K | Wacker, D | Wang, S | Antipsychotic | D2 | Dopamine receptor | Gpcr | Membrane protein | Risperidone
