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TitleLigand recognition and allosteric regulation of DRD1-Gs signaling complexes.
Journal, issue, pagesCell, Vol. 184, Issue 4, Page 943-956.e18, Year 2021
Publish dateFeb 18, 2021
AuthorsPeng Xiao / Wei Yan / Lu Gou / Ya-Ni Zhong / Liangliang Kong / Chao Wu / Xin Wen / Yuan Yuan / Sheng Cao / Changxiu Qu / Xin Yang / Chuan-Cheng Yang / Anjie Xia / Zhenquan Hu / Qianqian Zhang / Yong-Hao He / Dao-Lai Zhang / Chao Zhang / Gui-Hua Hou / Huanxiang Liu / Lizhe Zhu / Ping Fu / Shengyong Yang / Daniel M Rosenbaum / Jin-Peng Sun / Yang Du / Lei Zhang / Xiao Yu / Zhenhua Shao /
PubMed AbstractDopamine receptors, including D1- and D2-like receptors, are important therapeutic targets in a variety of neurological syndromes, as well as cardiovascular and kidney diseases. Here, we present five ...Dopamine receptors, including D1- and D2-like receptors, are important therapeutic targets in a variety of neurological syndromes, as well as cardiovascular and kidney diseases. Here, we present five cryoelectron microscopy (cryo-EM) structures of the dopamine D1 receptor (DRD1) coupled to Gs heterotrimer in complex with three catechol-based agonists, a non-catechol agonist, and a positive allosteric modulator for endogenous dopamine. These structures revealed that a polar interaction network is essential for catecholamine-like agonist recognition, whereas specific motifs in the extended binding pocket were responsible for discriminating D1- from D2-like receptors. Moreover, allosteric binding at a distinct inner surface pocket improved the activity of DRD1 by stabilizing endogenous dopamine interaction at the orthosteric site. DRD1-Gs interface revealed key features that serve as determinants for G protein coupling. Together, our study provides a structural understanding of the ligand recognition, allosteric regulation, and G protein coupling mechanisms of DRD1.
External linksCell / PubMed:33571432 / PubMed Central
MethodsEM (single particle)
Resolution3.1 - 3.54 Å
Structure data

30392

7ckw

EMDB-30392: Cryo-EM structure of Fenoldopam bound dopamine receptor DRD1-Gs signaling complex.
PDB-7ckw: Cryo-EM structure of Fenoldopam bound dopamine receptor DRD1-Gs signaling complex
Method: EM (single particle) / Resolution: 3.22 Å

30393

7ckx

EMDB-30393, PDB-7ckx:
Cryo-EM structure of A77636 bound dopamine receptor DRD1-Gs signaling complex
Method: EM (single particle) / Resolution: 3.54 Å

30394

7cky

EMDB-30394, PDB-7cky:
Cryo-EM structure of PW0464 bound dopamine receptor DRD1-Gs signaling complex
Method: EM (single particle) / Resolution: 3.2 Å

30395

7ckz

EMDB-30395, PDB-7ckz:
Cryo-EM structure of Dopamine and LY3154207 bound dopamine receptor DRD1-Gs signaling complex
Method: EM (single particle) / Resolution: 3.1 Å

30452

7crh

EMDB-30452, PDB-7crh:
Cryo-EM structure of SKF83959 bound dopamine receptor DRD1-Gs signaling complex
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-G3C:
(1R)-6-chloranyl-1-(4-hydroxyphenyl)-2,3,4,5-tetrahydro-1H-3-benzazepine-7,8-diol

ChemComp-CLR:
CHOLESTEROL

ChemComp-G3O:
(1R,3S)-3-(1-adamantyl)-1-(aminomethyl)-3,4-dihydro-1H-isochromene-5,6-diol

ChemComp-G3U:
6-[4-[3-[bis(fluoranyl)methoxy]pyridin-2-yl]oxy-2-methyl-phenyl]-1,5-dimethyl-pyrimidine-2,4-dione

ChemComp-LDP:
L-DOPAMINE / medication*YM

ChemComp-G4C:
2-[2,6-bis(chloranyl)phenyl]-1-[(1S,3R)-3-(hydroxymethyl)-1-methyl-5-(3-methyl-3-oxidanyl-butyl)-3,4-dihydro-1H-isoquinolin-2-yl]ethanone

ChemComp-GBU:
(1S)-6-chloranyl-3-methyl-1-(3-methylphenyl)-1,2,4,5-tetrahydro-3-benzazepine-7,8-diol

Source
  • homo sapiens (human)
  • lama glama (llama)
KeywordsCELL CYCLE / transmembrane protein / signaling transduction / transduction / complex / signaling complex / cell signaling

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