Evidence map›Paper›PMID 29968676›Full record

ArticleActa crystallographica. Section D, Structural biology2018

Crystal structures of two tandem malectin-like receptor kinases involved in plant reproduction.

Steven Moussu, Sebastian Augustin, Andra Octavia Roman, Caroline Broyart, Julia Santiago

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Acta crystallographica. Section D, Structural biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.6field-weighted citation impact, top 9% 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

27 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
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  7. Why is FERONIA pleiotropic?Nature plants · 2023
    Review
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  9. Article
  10. Article
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  14. Review
  15. Article
  16. Review
  17. Crystal structure of the extracellular domain of the receptor-like kinase TMK3 from Arabidopsis thaliana.Acta crystallographica. Section F, Structural biology communications · 2020
    Article
  18. Review
  19. Structural basis for recognition of RALF peptides by LRX proteins during pollen tube growth.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  20. 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

5 authors at 1 institution in 1 country.

Steven MoussuThe Plant Signaling Mechanisms Laboratory, Department of Plant Molecular Biology, University of Lausanne, 1015 Lausanne, Switzerland.
Sebastian AugustinThe Plant Signaling Mechanisms Laboratory, Department of Plant Molecular Biology, University of Lausanne, 1015 Lausanne, Switzerland.
Andra Octavia RomanThe Plant Signaling Mechanisms Laboratory, Department of Plant Molecular Biology, University of Lausanne, 1015 Lausanne, Switzerland.
Caroline BroyartThe Plant Signaling Mechanisms Laboratory, Department of Plant Molecular Biology, University of Lausanne, 1015 Lausanne, Switzerland.
Julia SantiagoThe Plant Signaling Mechanisms Laboratory, Department of Plant Molecular Biology, University of Lausanne, 1015 Lausanne, Switzerland.
University of Lausanne · CH

Funding

EMBO ALTF 1004-2017H2020 European Research Council 716358Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung 31003A_173101Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung PZ00P3_161534
6 · The paper itself

Abstract

Complex cell-to-cell communication between the male pollen tube and the female reproductive organs is required for plant fertilization. A family of Catharanthus roseus receptor kinase 1-like (CrRLK1L) membrane receptors has been genetically implicated in this process. Here, crystal structures of the CrRLK1Ls ANXUR1 and ANXUR2 are reported at 1.48 and 1.1 Å resolution, respectively. The structures reveal a novel arrangement of two malectin-like domains connected by a short β-hairpin linker and stabilized by calcium ions. The canonical carbohydrate-interaction surfaces of related animal and bacterial carbohydrate-binding modules are not conserved in plant CrRLK1Ls. In line with this, the binding of chemically diverse oligosaccharides to ANXUR1 and HERCULES1 could not be detected. Instead, CrRLK1Ls have evolved a protein-protein interface between their malectin domains which forms a deep cleft lined by highly conserved aromatic and polar residues. Analysis of the glycosylation patterns of different CrRLK1Ls and their oligomeric states suggests that this cleft could resemble a binding site for a ligand required for receptor activation of CrRLK1Ls.

Indexed as

ReproductionArabidopsis ProteinsBinding SitesCalciumCatharanthusCrystallography, X-RayGlycosylationPlant ProteinsProtein ConformationProtein DomainsProtein Interaction Domains and MotifsProtein KinasesANXUR1 protein, ArabidopsisANXUR2 protein, ArabidopsisArabidopsis ProteinsCalciumPlant ProteinsProtein KinasesArabidopsisCatharanthus roseuscell signallingcell-wall signallingmalectin-like receptor kinasesmembrane receptorsmembrane signallingplant reproductive signallingreceptor kinases

Identifiers

PMID29968676
PMCPMC6038381
OpenAlexW2789017703

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.