Ligand recognition and biased agonism of the D1 dopamine receptor.


Journal

Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555

Informations de publication

Date de publication:
08 06 2022
Historique:
received: 18 10 2021
accepted: 25 05 2022
entrez: 8 6 2022
pubmed: 9 6 2022
medline: 11 6 2022
Statut: epublish

Résumé

Dopamine receptors are widely distributed in the central nervous system and are important therapeutic targets for treatment of various psychiatric and neurological diseases. Here, we report three cryo-electron microscopy structures of the D1 dopamine receptor (D1R)-Gs complex bound to two agonists, fenoldopam and tavapadon, and a positive allosteric modulator LY3154207. The structure reveals unusual binding of two fenoldopam molecules, one to the orthosteric binding pocket (OBP) and the other to the extended binding pocket (EBP). In contrast, one elongated tavapadon molecule binds to D1R, extending from OBP to EBP. Moreover, LY3154207 stabilizes the second intracellular loop of D1R in an alpha helical conformation to efficiently engage the G protein. Through a combination of biochemical, biophysical and cellular assays, we further show that the broad conformation stabilized by two fenoldopam molecules and interaction between TM5 and the agonist are important for biased signaling of D1R.

Identifiants

pubmed: 35676276
doi: 10.1038/s41467-022-30929-w
pii: 10.1038/s41467-022-30929-w
pmc: PMC9177848
doi:

Substances chimiques

Dopamine Agonists 0
Ligands 0
Receptors, Dopamine D1 0
Fenoldopam INU8H2KAWG
Dopamine VTD58H1Z2X

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

3186

Informations de copyright

© 2022. The Author(s).

Références

Nat Commun. 2021 Jun 3;12(1):3305
pubmed: 34083522
Cell. 2019 Jan 24;176(3):468-478.e11
pubmed: 30639099
Science. 2019 Jun 28;364(6447):1283-1287
pubmed: 31249059
Science. 2017 Oct 20;358(6361):381-386
pubmed: 29051383
Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):213-21
pubmed: 20124702
Am J Med. 1984 Oct 5;77(4A):37-44
pubmed: 6148892
Nat Commun. 2020 Mar 2;11(1):1145
pubmed: 32123179
Cell. 2021 Feb 18;184(4):943-956.e18
pubmed: 33571432
ACS Med Chem Lett. 2019 Apr 05;10(5):792-799
pubmed: 31098001
Cell. 2021 Feb 18;184(4):931-942.e18
pubmed: 33571431
Neuropharmacology. 2014 Nov;86:145-54
pubmed: 24929112
Clin Neuropharmacol. 1998 Nov-Dec;21(6):339-43
pubmed: 9844789
Cell. 2019 May 16;177(5):1217-1231.e18
pubmed: 31006530
Elife. 2019 Nov 21;8:
pubmed: 31750832
Cell Res. 2021 May;31(5):593-596
pubmed: 33750903
Front Biol (Beijing). 2015 Jun;10(3):230-238
pubmed: 28280503
Br J Pharmacol. 2015 Jan;172(1):1-23
pubmed: 25671228
Mol Psychiatry. 2004 May;9(5):500-9
pubmed: 14569274
Eur J Pharmacol. 1983 Jul 15;91(1):153-4
pubmed: 6225651
Front Psychiatry. 2014 May 19;5:47
pubmed: 24904434
J Comput Chem. 2004 Oct;25(13):1605-12
pubmed: 15264254
Nature. 2020 Aug;584(7819):125-129
pubmed: 32528175
Nat Methods. 2017 Mar;14(3):290-296
pubmed: 28165473
Chem Rev. 2017 Jan 11;117(1):139-155
pubmed: 27622975
Bioorg Med Chem Lett. 2021 Jan 1;31:127696
pubmed: 33221389
Acta Crystallogr D Biol Crystallogr. 2010 Jan;66(Pt 1):12-21
pubmed: 20057044
ACS Chem Neurosci. 2015 Apr 15;6(4):681-92
pubmed: 25660762
Nature. 1957 Nov 30;180(4596):1200
pubmed: 13483658
Signal Transduct Target Ther. 2021 May 22;6(1):205
pubmed: 34023856
Eur J Pharmacol. 1996 Aug 1;309(1):13-20
pubmed: 8864687
Pharmacol Rev. 2011 Mar;63(1):182-217
pubmed: 21303898
Nat Commun. 2018 Feb 14;9(1):674
pubmed: 29445200
Nat Methods. 2015 Oct;12(10):943-6
pubmed: 26280328
Nature. 2011 Jul 19;477(7366):549-55
pubmed: 21772288
J Med Chem. 2019 Jan 10;62(1):128-140
pubmed: 30525590
Mol Cell. 2021 Mar 18;81(6):1147-1159.e4
pubmed: 33548201
Nature. 2013 Dec 5;504(7478):101-6
pubmed: 24256733
Nat Struct Mol Biol. 2015 May;22(5):362-9
pubmed: 25895059
Mol Pharmacol. 2011 Sep;80(3):367-77
pubmed: 21610196
Nature. 2018 Mar 8;555(7695):269-273
pubmed: 29466326
Science. 2010 Nov 19;330(6007):1091-5
pubmed: 21097933
Science. 1958 Feb 28;127(3296):471
pubmed: 13529006
Med Res Rev. 2009 Mar;29(2):272-94
pubmed: 18642350
J Biol Chem. 2018 May 11;293(19):7466-7473
pubmed: 29523687
Nature. 2020 Jul;583(7818):862-866
pubmed: 32555462
J Med Chem. 2019 Apr 11;62(7):3753-3772
pubmed: 30875219
Nat Commun. 2020 Feb 26;11(1):1074
pubmed: 32103023
Cell. 2019 Jun 13;177(7):1933-1947.e25
pubmed: 31160049
Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2126-32
pubmed: 15572765
ACS Chem Neurosci. 2019 Sep 18;10(9):4160-4182
pubmed: 31387346
Neurol Ther. 2018 Dec;7(2):307-319
pubmed: 30361858
Nature. 2019 Mar;567(7746):127-131
pubmed: 30814734
Int J Med Chem. 2011;2011:403039
pubmed: 25954517
Clin Pharmacol Drug Dev. 2021 Apr;10(4):393-403
pubmed: 33029934
Nat Struct Mol Biol. 2018 Jan;25(1):4-12
pubmed: 29323277
Methods. 2013 Mar;59(3):301-15
pubmed: 23270813
Curr Opin Cell Biol. 2014 Apr;27:136-43
pubmed: 24534489
Physiol Rev. 1998 Jan;78(1):189-225
pubmed: 9457173
Nat Methods. 2017 Apr;14(4):331-332
pubmed: 28250466
Adv Pharmacol. 2019;86:273-305
pubmed: 31378255
N Engl J Med. 2001 Nov 22;345(21):1548-57
pubmed: 11794223
Int J Mol Sci. 2021 Feb 16;22(4):
pubmed: 33669406
Sci Adv. 2022 Jun 10;8(23):eabo4158
pubmed: 35687690

Auteurs

Xiao Teng (X)

Tsinghua Institute of Multidisciplinary Biomedical Research, Tsinghua University, Beijing, China.
National Institute of Biological Sciences, Beijing, China.

Sijia Chen (S)

National Institute of Biological Sciences, Beijing, China.
Graduate School of Peking Union Medical College, Beijing, China.

Yingying Nie (Y)

National Institute of Biological Sciences, Beijing, China.

Peng Xiao (P)

Key Laboratory Experimental Teratology of the Ministry of Education and Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Cheeloo College of Medicine, Shandong University, Jinan, Shandong, China.

Xiao Yu (X)

Key Laboratory Experimental Teratology of the Ministry of Education and Department of Physiology, School of Basic Medical Sciences, Cheeloo College of Medicine, Shandong University, Jinan, Shandong, China.

Zhenhua Shao (Z)

Division of Nephrology and Kidney Research Institute, State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan University, Chengdu, Sichuan, China.

Sanduo Zheng (S)

Tsinghua Institute of Multidisciplinary Biomedical Research, Tsinghua University, Beijing, China. zhengsanduo@nibs.ac.cn.
National Institute of Biological Sciences, Beijing, China. zhengsanduo@nibs.ac.cn.
Graduate School of Peking Union Medical College, Beijing, China. zhengsanduo@nibs.ac.cn.

Articles similaires

Photosynthesis Ribulose-Bisphosphate Carboxylase Carbon Dioxide Molecular Dynamics Simulation Cyanobacteria
Receptor, Cannabinoid, CB1 Ligands Molecular Dynamics Simulation Protein Binding Thermodynamics
Cryoelectron Microscopy Algorithms Image Processing, Computer-Assisted Consensus Software

Amyloid accelerator polyphosphate fits as the mystery density in α-synuclein fibrils.

Philipp Huettemann, Pavithra Mahadevan, Justine Lempart et al.
1.00
Polyphosphates alpha-Synuclein Humans Amyloid Molecular Dynamics Simulation

Classifications MeSH