Evidence map›Paper›PMID 20566411›Full record

ArticleJournal of molecular biology2010

Crystal structure of the GalNAc/Gal-specific agglutinin from the phytopathogenic ascomycete Sclerotinia sclerotiorum reveals novel adaptation of a beta-trefoil domain.

Gerlind Sulzenbacher, Véronique Roig-Zamboni, Willy J Peumans, Pierre Rougé, Els J M Van Damme, Yves Bourne

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

13 citing papers in PubMed, 36 citations in OpenAlex.

  1. Journal of fungi (Basel, Switzerland) · 2023
    Article
  2. Article
  3. CNL-Molecules (Basel, Switzerland) · 2019
    Review
  4. Article
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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

6 authors at 4 institutions in 2 countries.

Gerlind SulzenbacherArchitecture et Fonction des Macromolécules Biologiques UMR-6098 CNRS, Université Aix-Marseille, Campus Luminy, Case 932, F-13288 Marseille cedex 09, France.
Véronique Roig-Zamboni
Willy J Peumans
Pierre Rougé
Els J M Van Damme
Yves Bourne
Architecture et Fonction des Macromolécules Biologiques · FRCentre National de la Recherche Scientifique · FRGhent University · BEGhent University Hospital · BE

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

A lectin from the phytopathogenic ascomycete Sclerotinia sclerotiorum that shares only weak sequence similarity with characterized fungal lectins has recently been identified. S. sclerotiorum agglutinin (SSA) is a homodimeric protein consisting of two identical subunits of approximately 17 kDa and displays specificity primarily towards Gal/GalNAc. Glycan array screening indicates that SSA readily interacts with Gal/GalNAc-bearing glycan chains. The crystal structures of SSA in the ligand-free form and in complex with the Gal-beta1,3-GalNAc (T-antigen) disaccharide have been determined at 1.6 and 1.97 A resolution, respectively. SSA adopts a beta-trefoil domain as previously identified for other carbohydrate-binding proteins of the ricin B-like lectin superfamily and accommodates terminal non-reducing galactosyl and N-acetylgalactosaminyl glycans. Unlike other structurally related lectins, SSA contains a single carbohydrate-binding site at site alpha. SSA reveals a novel dimeric assembly markedly dissimilar to those described earlier for ricin-type lectins. The present structure exemplifies the adaptability of the beta-trefoil domain in the evolution of fungal lectins.

Indexed as

AgglutininsAmino Acid SequenceAntigens, Tumor-Associated, CarbohydrateAscomycotaBinding SitesCrystallography, X-RayDimerizationFungal ProteinsModels, MolecularMolecular Sequence DataProtein BindingProtein Structure, QuaternaryProtein Structure, TertiarySequence AlignmentAgglutininsAntigens, Tumor-Associated, CarbohydrateFungal ProteinsThomsen-Friedenreich antigen

Identifiers

PMID20566411
PMCPMC2956877
OpenAlexW2057342848

What OpenQuestion holds

Textmetadata
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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.