Evidence map›Paper›PMID 27524201›Full record

ArticleStructure (London, England : 1993)2016

Structure of the Dual-Mode Wnt Regulator Kremen1 and Insight into Ternary Complex Formation with LRP6 and Dickkopf.

Matthias Zebisch, Verity A Jackson, Yuguang Zhao, E Yvonne Jones

Open access · hybridAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

25 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Crystal structure of human Dickkopf 4 cysteine-rich domain 1 and evaluation of conformational rigidity.Acta crystallographica. Section F, Structural biology communications · 2026
    Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. LRPs in WNT Signalling.Handbook of experimental pharmacology · 2021
    Review
  16. The structural biology of canonical Wnt signalling.Biochemical Society transactions · 2020
    Review
  17. Molecular basis of Coxsackievirus A10 entry using the two-in-one attachment and uncoating receptor KRM1.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  18. Article
  19. Article
  20. MicroRNA-154 Targets the Wnt/β-Catenin Signaling Pathway Following Injury to Human Vascular Endothelial Cells by Hydrogen Peroxide.Medical science monitor : international medical journal of experimental and clinical research · 2019
    Article
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

4 authors at 2 institutions in 1 country.

Matthias ZebischDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, UK. Electronic address: matthias.zebisch@evotec.com.
Verity A JacksonDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, UK.
Yuguang ZhaoDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, UK.
E Yvonne JonesDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, UK. Electronic address: yvonne@strubi.ox.ac.uk.
Centre for Human Genetics · GBUniversity of Oxford · GB

Funding

Cancer Research UK 10976Cancer Research UK 17721Cancer Research UK A10976Medical Research Council G9900061Medical Research Council MR/M000141/1Wellcome Trust 090532/Z/09/Z
6 · The paper itself

Abstract

Kremen 1 and 2 have been identified as co-receptors for Dickkopf (Dkk) proteins, hallmark secreted antagonists of canonical Wnt signaling. We present here three crystal structures of the ectodomain of human Kremen1 (KRM1ECD) at resolutions between 1.9 and 3.2 Å. KRM1ECD emerges as a rigid molecule with tight interactions stabilizing a triangular arrangement of its Kringle, WSC, and CUB structural domains. The structures reveal an unpredicted homology of the WSC domain to hepatocyte growth factor. We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between β-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD. DKK1CRD2 is sandwiched between LRP6PE3 and KRM1Kringle-WSC. Modeling studies supported by surface plasmon resonance suggest a direct interaction site between Krm1CUB and Lrp6PE2.

Indexed as

Amino Acid MotifsBinding SitesCloning, MolecularCrystallography, X-RayGene ExpressionHEK293 CellsHumansIntercellular Signaling Peptides and ProteinsLow Density Lipoprotein Receptor-Related Protein-6Membrane ProteinsModels, MolecularProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsProtein MultimerizationDKK1 protein, humanIntercellular Signaling Peptides and ProteinsKREMEN1 protein, humanLow Density Lipoprotein Receptor-Related Protein-6LRP6 protein, humanMembrane ProteinsRecombinant Proteins

Identifiers

PMID27524201
PMCPMC5014086
OpenAlexW2508915320

What OpenQuestion holds

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LicenceCC BY
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.