Evidence map›Paper›PMID 18687680›Full record

ArticleThe Journal of biological chemistry2008

High affinity interaction between a bivalve C-type lectin and a biantennary complex-type N-glycan revealed by crystallography and microcalorimetry.

Jean-Philippe Gourdine, Gianluca Cioci, Laurence Miguet, Carlo Unverzagt, Daniel Varón Silva, Annabelle Varrot, Catherine Gautier, Emilie Juliette Smith-Ravin, Anne Imberty

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed, 1 pooled it
1.5field-weighted citation impact, top 18% 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

22 citing papers in PubMed, 1 synthesis or guideline pooled it, 42 citations in OpenAlex.

  1. Pooled it
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  14. Structural analysis for glycolipid recognition by the C-type lectins Mincle and MCL.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
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  17. Antibody WN1 222-5 mimics Toll-like receptor 4 binding in the recognition of LPS.Proceedings of the National Academy of Sciences of the United States of America · 2012
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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

9 authors at 4 institutions in 2 countries.

Jean-Philippe GourdineDépartement de Biologie, Université des Antilles et de la Guyane, Pointe-à-Pitre, F-97159 Guadeloupe, France.
Gianluca Cioci
Laurence Miguet
Carlo Unverzagt
Daniel Varón Silva
Annabelle Varrot
Catherine Gautier
Emilie Juliette Smith-Ravin
Anne Imberty
Centre National de la Recherche Scientifique · FRUniversité Joseph Fourier · FRUniversity of Bayreuth · DECEA Grenoble · FR

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

Codakine is an abundant 14-kDa mannose-binding C-type lectin isolated from the gills of the sea bivalve Codakia orbicularis. Binding studies using inhibition of hemagglutination indicated specificity for mannose and fucose monosaccharides. Further experiments using a glycan array demonstrated, however, a very fine specificity for N-linked biantennary complex-type glycans. An unusually high affinity was measured by titration microcalorimetry performed with a biantennary Asn-linked nonasaccharide. The crystal structure of the native lectin at 1.3A resolution revealed a new type of disulfide-bridged homodimer. Each monomer displays three intramolecular disulfide bridges and contains only one calcium ion located in the canonical binding site that is occupied by a glycerol molecule. The structure of the complex between Asn-linked nonasaccharide and codakine has been solved at 1.7A resolution. All residues could be located in the electron density map, except for the capping beta1-4-linked galactosides. The alpha1-6-linked mannose binds to calcium by coordinating the O3 and O4 hydroxyl groups. The GlcNAc moiety of the alpha1,6 arm engages in several hydrogen bonds with the protein, whereas the GlcNAc on the other antenna is stacked against Trp(108), forming an extended binding site. This is the first structural report for a bivalve lectin.

Indexed as

Amino Acid SequenceAnimalsBivalviaCalorimetryCarbohydrate ConformationCarbohydrate SequenceCrystallography, X-RayDimerizationDisulfidesKineticsLectinsMolecular ConformationMolecular Sequence DataPolysaccharidesSequence Homology, Amino AcidDisulfidesLectinsPolysaccharides

Identifiers

PMID18687680
PMCPMC2662075
OpenAlexW2086972154

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.