Evidence map›Paper›PMID 29959397›Full record

ArticleScientific reports2018

Crystallization of a human galectin-3 variant with two ordered segments in the shortened N-terminal tail.

Andrea Flores-Ibarra, Sabine Vértesy, Francisco J Medrano, Hans-Joachim Gabius, Antonio Romero

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

33 citing papers in PubMed, 46 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Spatial N-glycan rearrangement on αNature communications · 2025
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  6. Endocytic Roles of Glycans on Proteins and Lipids.Cold Spring Harbor perspectives in biology · 2024
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  7. Article
  8. Selectively Modified Lactose andInternational journal of molecular sciences · 2023
    Article
  9. Review
  10. Article
  11. Review
  12. Review
  13. Review
  14. Article
  15. Review
  16. Article
  17. The marriage of chemokines and galectins as functional heterodimers.Cellular and molecular life sciences : CMLS · 2021
    Review
  18. Review
  19. Galectin-Glycan Interactions: Guidelines for Monitoring byChemistry (Weinheim an der Bergstrasse, Germany) · 2021
    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 2 institutions in 2 countries.

Andrea Flores-IbarraDepartment of Structural and Chemical Biology, Centro de Investigaciones Biológicas, CSIC, Ramiro de Maeztu 9, 28040, Madrid, Spain.
Sabine VértesyInstitute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University Munich, Veterinärstrabe 13, 80539, Munich, Germany.
Francisco J MedranoDepartment of Structural and Chemical Biology, Centro de Investigaciones Biológicas, CSIC, Ramiro de Maeztu 9, 28040, Madrid, Spain.
Hans-Joachim GabiusInstitute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University Munich, Veterinärstrabe 13, 80539, Munich, Germany. gabius@tiph.vetmed-uni-muenchen.de.
Antonio RomeroDepartment of Structural and Chemical Biology, Centro de Investigaciones Biológicas, CSIC, Ramiro de Maeztu 9, 28040, Madrid, Spain. romero@cib.csic.es.ORCID 0000-0002-6990-6973
Centro de Investigaciones Biológicas Margarita Salas · ESLudwig-Maximilians-Universität München · DE

Funding

EC | Seventh Framework Programme (European Union Seventh Framework Programme) 317297 (“GLYCOPHARM“)Ministry of Economy and Competitiveness | Consejo Superior de Investigaciones Científicas (Spanish National Research Council) BFU2016-77835-R
6 · The paper itself

Abstract

Among members of the family of adhesion/growth-regulatory galectins, galectin-3 (Gal-3) bears a unique modular architecture. A N-terminal tail (NT) consisting of the N-terminal segment (NTS) and nine collagen-like repeats is linked to the canonical lectin domain. In contrast to bivalent proto- and tandem-repeat-type galectins, Gal-3 is monomeric in solution, capable to self-associate in the presence of bi- to multivalent ligands, and the NTS is involved in cellular compartmentalization. Since no crystallographic information on Gal-3 beyond the lectin domain is available, we used a shortened variant with NTS and repeats VII-IX. This protein crystallized as tetramers with contacts between the lectin domains. The region from Tyr101 (in repeat IX) to Leu114 (in the CRD) formed a hairpin. The NTS extends the canonical β-sheet of F1-F5 strands with two new β-strands on the F face. Together, crystallographic and SAXS data reveal a mode of intramolecular structure building involving the highly flexible Gal-3's NT.

Indexed as

Sequence DeletionBinding SitesBlood ProteinsCrystallizationCrystallography, X-RayGalectin 3GalectinsHumansMutant ProteinsProtein BindingProtein DomainsProtein EngineeringProtein Structure, QuaternaryScattering, Small AngleBlood ProteinsGalectin 3GalectinsLGALS3 protein, humanMutant Proteins

Identifiers

PMID29959397
PMCPMC6026190
OpenAlexW2811407415

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Registered trials

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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.