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Structure of the D2 dopamine receptor bound to the atypical antipsychotic drug risperidone
Authors
A Manglik
AJ McCoy
+54 more
Anat Levit
B Webb
BL Roth
BL Roth
Brian K. Shoichet
Bryan L. Roth
C Missale
C Southan
CC Chambers
D Wacker
DA Shapiro
DA Sykes
Daniel Wacker
DJ Roberts
DK Grandy
DM Rosenbaum
DR Sibley
EY Chien
FJ Monsma Jr
HJ Motulsky
HY Meltzer
I Creese
J Li
J Pei
J Sadowski
JA Allen
JA Ballesteros
JA Ballesteros
JA Javitch
JD McCorvy
JM Beaulieu
JM Word
JR Bunzow
K Gallagher
K Palczewski
KA Sharp
M Caffrey
MM Mysinger
MM Mysinger
ND Volkow
P Emsley
P Seeman
PA Janssen
PC Hawkins
PD Adams
RB Free
RG Coleman
S Kapur
S Kapur
S Wang
SG Rasmussen
Sheng Wang
Tao Che
W Minor
Publication date
1 January 2018
Publisher
Nature Publishing Group
Doi
Cite
Abstract
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, and nausea and vomiting. The actions of dopamine are mediated by a family of five G-protein-coupled receptors. The D2 dopamine receptor (DRD2) is the primary target for both typical and atypical antipsychotic drugs, and for drugs used to treat Parkinson's disease. Unfortunately, many drugs that target DRD2 cause serious and potentially life-threatening side effects due to promiscuous activities against related receptors. Accordingly, a molecular understanding of the structure and function of DRD2 could provide a template for the design of safer and more effective medications. Here we report 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 highlights structural determinants that are essential for the actions of risperidone and related drugs at DRD2. © 2018 Macmillan Publishers Limited, part of Springer Nature. All rights reserved
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info:doi/10.1038%2Fnature25758
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