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Structure paper

TitleStructural insights into the human D1 and D2 dopamine receptor signaling complexes.
Journal, issue, pagesCell, Vol. 184, Issue 4, Page 931-942.e18, Year 2021
Publish dateFeb 18, 2021
AuthorsYouwen Zhuang / Peiyu Xu / Chunyou Mao / Lei Wang / Brian Krumm / X Edward Zhou / Sijie Huang / Heng Liu / Xi Cheng / Xi-Ping Huang / Dan-Dan Shen / Tinghai Xu / Yong-Feng Liu / Yue Wang / Jia Guo / Yi Jiang / Hualiang Jiang / Karsten Melcher / Bryan L Roth / Yan Zhang / Cheng Zhang / H Eric Xu /
PubMed AbstractThe D1- and D2-dopamine receptors (D1R and D2R), which signal through G and G, respectively, represent the principal stimulatory and inhibitory dopamine receptors in the central nervous system. D1R ...The D1- and D2-dopamine receptors (D1R and D2R), which signal through G and G, respectively, represent the principal stimulatory and inhibitory dopamine receptors in the central nervous system. D1R and D2R also represent the main therapeutic targets for Parkinson's disease, schizophrenia, and many other neuropsychiatric disorders, and insight into their signaling is essential for understanding both therapeutic and side effects of dopaminergic drugs. Here, we report four cryoelectron microscopy (cryo-EM) structures of D1R-G and D2R-G signaling complexes with selective and non-selective dopamine agonists, including two currently used anti-Parkinson's disease drugs, apomorphine and bromocriptine. These structures, together with mutagenesis studies, reveal the conserved binding mode of dopamine agonists, the unique pocket topology underlying ligand selectivity, the conformational changes in receptor activation, and potential structural determinants for G protein-coupling selectivity. These results provide both a molecular understanding of dopamine signaling and multiple structural templates for drug design targeting the dopaminergic system.
External linksCell / PubMed:33571431 / PubMed Central
MethodsEM (single particle)
Resolution2.8 - 3.0 Å
Structure data

22493

7jv5

EMDB-22493, PDB-7jv5:
Cryo-EM structure of SKF-81297-bound dopamine receptor 1 in complex with Gs protein
Method: EM (single particle) / Resolution: 3.0 Å

22509

7jvp

EMDB-22509, PDB-7jvp:
Cryo-EM structure of SKF-83959-bound dopamine receptor 1 in complex with Gs protein
Method: EM (single particle) / Resolution: 2.9 Å

22510

7jvq

EMDB-22510, PDB-7jvq:
Cryo-EM structure of apomorphine-bound dopamine receptor 1 in complex with Gs protein
Method: EM (single particle) / Resolution: 3.0 Å

22511

7jvr

EMDB-22511, PDB-7jvr:
Cryo-EM structure of Bromocriptine-bound dopamine receptor 2 in complex with Gi protein
Method: EM (single particle) / Resolution: 2.8 Å

Chemicals

ChemComp-SK0:
(1R)-6-chloro-1-phenyl-2,3,4,5-tetrahydro-1H-3-benzazepine-7,8-diol

ChemComp-CLR:
CHOLESTEROL / Cholesterol

ChemComp-PLM:
PALMITIC ACID / Palmitic acid

ChemComp-SK9:
(1R)-6-chloro-3-methyl-1-(3-methylphenyl)-2,3,4,5-tetrahydro-1H-3-benzazepine-7,8-diol

ChemComp-OR9:
(6aR)-6-methyl-5,6,6a,7-tetrahydro-4H-dibenzo[de,g]quinoline-10,11-diol / antagonist*YM / Apomorphine

ChemComp-08Y:
bromoergocryptine / agonist*YM / Bromocriptine

Source
  • homo sapiens (human)
  • synthetic construct (others)
  • escherichia coli (E. coli)
KeywordsSIGNALING PROTEIN / Dopamine receptor 2 / Gi protein / SKF-81297 / Dopamine receptor 1 / SKF-83959 / apomorphine / bromocriptine

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