Evidence map›Paper›PMID 26828567›Full record

ArticleScientific reports2016

Structural characterisation of human galectin-4 N-terminal carbohydrate recognition domain in complex with glycerol, lactose, 3'-sulfo-lactose, and 2'-fucosyllactose.

Khuchtumur Bum-Erdene, Hakon Leffler, Ulf J Nilsson, Helen Blanchard

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 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
1.9field-weighted citation impact, top 15% 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, 47 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. A brief history of galectin evolution.Frontiers in immunology · 2023
    Article
  10. 3'-sulfated LewisFrontiers in cell and developmental biology · 2023
    Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Synthesis of Galectin Inhibitors by Regioselective 3'-Molecules (Basel, Switzerland) · 2020
    Article
  16. Review
  17. Article
  18. Article
  19. Exploring functional pairing between surface glycoconjugates and human galectins using programmable glycodendrimersomes.Proceedings of the National Academy of Sciences of the United States of America · 2018
    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

4 authors at 2 institutions in 2 countries.

Khuchtumur Bum-ErdeneInstitute for Glycomics, Griffith University, Gold Coast Campus, Queensland 4222, Australia.
Hakon LefflerSection MIG, Department of Laboratory Medicine, Lund University, BMC-C1228b, Klinikgatan 28, SE-22184 Lund, Sweden.
Ulf J NilssonCentre for Analysis and Synthesis, Department of Chemistry, Lund University, PO Box 124, SE-22100 Lund, Sweden.
Helen BlanchardInstitute for Glycomics, Griffith University, Gold Coast Campus, Queensland 4222, Australia.
Griffith University · AULund University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Galectin-4 is a tandem-repeat galectin with two distinct carbohydrate recognition domains (CRD). Galectin-4 is expressed mainly in the alimentary tract and is proposed to function as a lipid raft and adherens junction stabilizer by its glycan cross-linking capacity. Galectin-4 plays divergent roles in cancer and inflammatory conditions, either promoting or inhibiting each disease progression, depending on the specific pathological condition. The study of galectin-4's ligand-binding profile may help decipher its roles under specific conditions. Here we present the X-ray structures of human galectin-4 N-terminal CRD (galectin-4N) bound to different saccharide ligands. Galectin-4's overall fold and its core interactions to lactose are similar to other galectin CRDs. Galectin-4N recognises the sulfate cap of 3'-sulfated glycans by a weak interaction through Arg45 and two water-mediated hydrogen bonds via Trp84 and Asn49. When galectin-4N interacts with the H-antigen mimic, 2'-fucosyllactose, an interaction is formed between the ring oxygen of fucose and Arg45. The extended binding site of galectin-4N may not be well suited to the A/B-antigen determinants, α-GalNAc/α-Gal, specifically due to clashes with residue Phe47. Overall, galectin-4N favours sulfated glycans whilst galectin-4C prefers blood group determinants. However, the two CRDs of galectin-4 can, to a less extent, recognise each other's ligands.

Indexed as

Models, MolecularMolecular ConformationProtein Interaction Domains and MotifsGalectin 4GlycerolHumansLactoseProtein BindingTrisaccharides2'-fucosyllactoseGalectin 4GlycerolLactoseTrisaccharides

Identifiers

PMID26828567
PMCPMC4734333
OpenAlexW2290586294

What OpenQuestion holds

Textmetadata
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.