Evidence map›Paper›PMID 18440554›Full record

ArticleJournal of molecular biology2008

Structural basis for chitotetraose coordination by CGL3, a novel galectin-related protein from Coprinopsis cinerea.

Martin Andreas Wälti, Piers Jamie Walser, Stéphane Thore, Anke Grünler, Michaela Bednar, Markus Künzler, Markus Aebi

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed, 1 pooled it
2.2field-weighted citation impact, top 13% 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

28 citing papers in PubMed, 1 synthesis or guideline pooled it, 61 citations in OpenAlex.

  1. Pooled it
  2. The Entomotoxic Fungal LectinJournal of agricultural and food chemistry · 2026
    Article
  3. Article
  4. Modulation ofFrontiers in cellular and infection microbiology · 2024
    Article
  5. Article
  6. International journal of molecular sciences · 2022
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Lectins from edible mushrooms.Molecules (Basel, Switzerland) · 2014
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. LEC-2, a highly variable lectin in the lichenSymbiosis (Philadelphia, Pa.) · 2012
    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

7 authors at 2 institutions in 2 countries.

Martin Andreas WältiInstitute of Microbiology, ETH Zürich, Wolfgang-Pauli-Str. 10, CH-8093 Zürich, Switzerland.
Piers Jamie Walser
Stéphane Thore
Anke Grünler
Michaela Bednar
Markus Künzler
Markus Aebi
ETH Zurich · CHUniversity of Queensland · AU

Funding

Structural Basis of Immune Recognition of Glycosylated AntigensU54GM062116 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI SASISEKHARAN, RAM · 2001 to 2010
$80.3M
NIGMS NIH HHS GM62116NIGMS NIH HHS U54 GM062116
6 · The paper itself

Abstract

Recent advances in genome sequencing efforts have revealed an abundance of novel putative lectins. Among these, many galectin-related proteins, characterized by many conserved residues but intriguingly lacking critical amino acids, have been found in all corners of the eukaryotic superkingdom. Here we present a structural and biochemical analysis of one representative, the galectin-related lectin CGL3 found in the inky cap mushroom Coprinopsis cinerea. This protein contains all but one conserved residues known to be involved in beta-galactoside binding in galectins. A Trp residue strictly conserved among galectins is changed to an Arg in CGL3 (R81). Accordingly, the galectin-related protein is not able to bind lactose. Screening of a glycan array revealed that CGL3 displays preference for oligomers of beta1-4-linked N-acetyl-glucosamines (chitooligosaccharides) and GalNAc beta 1-4GlcNAc (LacdiNAc). Carbohydrate-binding affinity of this novel lectin was quantified using isothermal titration calorimetry, and its mode of chitooligosaccharide coordination not involving any aromatic amino acid residues was studied by X-ray crystallography. Structural information was used to alter the carbohydrate-binding specificity and substrate affinity of CGL3. The importance of residue R81 in determining the carbohydrate-binding specificity was demonstrated by replacing this Arg with a Trp residue (R81W). This single-amino-acid change led to a lectin that failed to bind chitooligosaccharides but gained lactose binding. Our results demonstrate that, similar to the legume lectin fold, the galectin fold represents a conserved structural framework upon which dramatically altered specificities can be grafted by few alterations in the binding site and that, in consequence, many metazoan galectin-related proteins may represent lectins with novel carbohydrate-binding specificities.

Indexed as

AgaricalesAmino Acid SequenceAmino Acid SubstitutionConserved SequenceFungal ProteinsGalectin 2Galectin 3Molecular Sequence DataOligosaccharidesProtein ConformationProtein FoldingThermodynamicschitotetroseFungal ProteinsGalectin 2Galectin 3Oligosaccharides

Identifiers

PMID18440554
PMCPMC2785874
OpenAlexW2013973057

What OpenQuestion holds

Textmetadata
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.