Evidence map›Paper›PMID 27152332›Full record

ArticleScience advances2016

The crystal structure of human dopamine β-hydroxylase at 2.9 Å resolution.

Trine V Vendelboe, Pernille Harris, Yuguang Zhao, Thomas S Walter, Karl Harlos, Kamel El Omari, Hans E M Christensen

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
7.0field-weighted citation impact, top 3% 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

57 citing papers in PubMed, 116 citations in OpenAlex.

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  8. Associations Between Dopamine Beta-Hydroxylase Gene Polymorphisms and Restless Legs Syndrome: A Case-Control Study.Medical science monitor : international medical journal of experimental and clinical research · 2025
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  10. Electron transfer in polysaccharide monooxygenase catalysis.Proceedings of the National Academy of Sciences of the United States of America · 2025
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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

7 authors at 2 institutions in 2 countries.

Trine V VendelboeDepartment of Chemistry, Kemitorvet 207, Technical University of Denmark, DK-2800 Kgs. Lyngby, Denmark.
Pernille HarrisDepartment of Chemistry, Kemitorvet 207, Technical University of Denmark, DK-2800 Kgs. Lyngby, Denmark.ORCID 0000-0002-6806-4903
Yuguang ZhaoDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, UK.ORCID 0000-0001-8916-8552
Thomas S WalterDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, UK.ORCID 0000-0002-0030-7235
Karl HarlosDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, UK.ORCID 0000-0002-7266-4354
Kamel El OmariDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, UK.ORCID 0000-0003-3506-6045
Hans E M ChristensenDepartment of Chemistry, Kemitorvet 207, Technical University of Denmark, DK-2800 Kgs. Lyngby, Denmark.ORCID 0000-0002-9540-8679
Centre for Human Genetics · GBTechnical University of Denmark · DK

Funding

Medical Research Council G1100525Medical Research Council MR/N00065X/1Wellcome TrustWellcome Trust 075491/Z/04
6 · The paper itself

Abstract

The norepinephrine pathway is believed to modulate behavioral and physiological processes, such as mood, overall arousal, and attention. Furthermore, abnormalities in the pathway have been linked to numerous diseases, for example hypertension, depression, anxiety, Parkinson's disease, schizophrenia, Alzheimer's disease, attention deficit hyperactivity disorder, and cocaine dependence. We report the crystal structure of human dopamine β-hydroxylase, which is the enzyme converting dopamine to norepinephrine. The structure of the DOMON (dopamine β-monooxygenase N-terminal) domain, also found in >1600 other proteins, reveals a possible metal-binding site and a ligand-binding pocket. The catalytic core structure shows two different conformations: an open active site, as also seen in another member of this enzyme family [the peptidylglycine α-hydroxylating (and α-amidating) monooxygenase], and a closed active site structure, in which the two copper-binding sites are only 4 to 5 Å apart, in what might be a coupled binuclear copper site. The dimerization domain adopts a conformation that bears no resemblance to any other known protein structure. The structure provides new molecular insights into the numerous devastating disorders of both physiological and neurological origins associated with the dopamine system.

Indexed as

Protein ConformationBinding SitesCatalytic DomainCopperCrystallography, X-RayDopamineDopamine beta-HydroxylaseHumansNorepinephrineCopperDopamineDopamine beta-HydroxylaseNorepinephrinebiochemistrybiomoleculescrystal structuredopaminedopamine β-hydroxylaseLife sciencesneurochemistrynorepinephrinestructural biology

Identifiers

PMID27152332
PMCPMC4846438
OpenAlexW2322161127

What OpenQuestion holds

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LicenceCC BY
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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.