Evidence map›Paper›PMID 34083522›Full record

ArticleNature communications2021

Crystal structure of dopamine D1 receptor in complex with G protein and a non-catechol agonist.

Bingfa Sun, Dan Feng, Matthew Ling-Hon Chu, Inbar Fish, Silvia Lovera, Zara A Sands, Sebastian Kelm, Anne Valade, Martyn Wood, Tom Ceska and 3 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed, 1 pooled it
3.5field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

32 citing papers in PubMed, 1 synthesis or guideline pooled it, 58 citations in OpenAlex.

  1. The Signaling and Pharmacology of the Dopamine D1 Receptor.Frontiers in cellular neuroscience · 2021
    Pooled it
  2. The structure of the dopamine DScience advances · 2026
    Article
  3. Review
  4. Pharmaceuticals (Basel, Switzerland) · 2025
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. G Protein-Coupled Receptor-Ligand Pose and Functional Class Prediction.International journal of molecular sciences · 2024
    Article
  12. Article
  13. Article
  14. Dopamine receptor divergence revealed using a common ligand.Trends in pharmacological sciences · 2023
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors at 3 institutions in 3 countries.

Bingfa Sun *ConfometRx, Inc., Santa Clara, CA, USA.ORCID http://orcid.org/0000-0001-5001-5065
Dan Feng *ConfometRx, Inc., Santa Clara, CA, USA.
Matthew Ling-Hon ChuConfometRx, Inc., Santa Clara, CA, USA.
Inbar FishConfometRx, Inc., Santa Clara, CA, USA.
Silvia LoveraUCB Pharma, Braine-l'Alleud, Belgium.
Zara A SandsUCB Pharma, Braine-l'Alleud, Belgium.
Sebastian KelmUCB Pharma, Slough, UK.ORCID http://orcid.org/0000-0001-7146-9322
Anne ValadeUCB Pharma, Braine-l'Alleud, Belgium.
Martyn WoodUCB Pharma, Braine-l'Alleud, Belgium.
Tom CeskaUCB Pharma, Slough, UK.ORCID http://orcid.org/0000-0002-7200-9528
Tong Sun KobilkaConfometRx, Inc., Santa Clara, CA, USA.
Florence LebonUCB Pharma, Anderlecht, Belgium.
Brian K KobilkaConfometRx, Inc., Santa Clara, CA, USA. kobilka@stanford.edu.ORCID http://orcid.org/0000-0001-5958-3990
ConfometRx (United States) · USUCB Pharma (Belgium) · BEUCB Pharma (United Kingdom) · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dopamine D1 receptor (D1R) is an important drug target implicated in many psychiatric and neurological disorders. Selective agonism of D1R are sought to be the therapeutic strategy for these disorders. Most selective D1R agonists share a dopamine-like catechol moiety in their molecular structure, and their therapeutic potential is therefore limited by poor pharmacological properties in vivo. Recently, a class of non-catechol D1R selective agonists with a distinct scaffold and pharmacological properties were reported. Here, we report the crystal structure of D1R in complex with stimulatory G protein (Gs) and a non-catechol agonist Compound 1 at 3.8 Å resolution. The structure reveals the ligand bound to D1R in an extended conformation, spanning from the orthosteric site to extracellular loop 2 (ECL2). Structural analysis reveals that the unique features of D1R ligand binding pocket explains the remarkable selectivity of this scaffold for D1R over other aminergic receptors, and sheds light on the mechanism for D1R activation by the non-catechol agonist.

Indexed as

Binding SitesCrystallography, X-RayGTP-Binding Protein alpha Subunits, GsHumansIn Vitro TechniquesLigandsModels, MolecularMolecular Dynamics SimulationProtein BindingProtein ConformationProtein EngineeringProtein Structure, QuaternaryReceptors, Dopamine D1Recombinant ProteinsDRD1 protein, humanGTP-Binding Protein alpha Subunits, GsLigandsReceptors, Dopamine D1Recombinant Proteins

Identifiers

PMID34083522
PMCPMC8175458
OpenAlexW3155515017

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.