Evidence map›Paper›PMID 21572446›Full record

ArticleNature structural & molecular biology2011

Molecular design principles underlying β-strand swapping in the adhesive dimerization of cadherins.

Jeremie Vendome, Shoshana Posy, Xiangshu Jin, Fabiana Bahna, Goran Ahlsen, Lawrence Shapiro, Barry Honig

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

54 citing papers in PubMed, 112 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Engineering the Interactions of Classical Cadherin Cell-Cell Adhesion Proteins.Journal of immunology (Baltimore, Md. : 1950) · 2023
    Review
  7. Antiparallel dimer structure of CELSR cadherin in solution revealed by high-speed atomic force microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  8. Article
  9. Molecular mechanism for strengthening E-cadherin adhesion using a monoclonal antibody.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  10. 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

7 authors at 2 institutions in 1 country.

Jeremie VendomeDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, New York, USA. Center for Computational Biology and Bioinformatics, Columbia University, New York, New York, USA. Howard Hughes Medical Institute, Columbia University, New York, New York, USA.
Shoshana Posy
Xiangshu Jin
Fabiana Bahna
Goran Ahlsen
Lawrence Shapiro
Barry Honig
Columbia University · USHoward Hughes Medical Institute · US

Funding

MOLECULAR BASIS OF CADHERIN MEDIATED CELL ADHESIONR01GM062270 · NIGMS · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI SHAPIRO, LAWRENCE S · 2001 to 2015
$3.4M
NIGMS NIH HHS R01 GM062270
6 · The paper itself

Abstract

Cell adhesion by classical cadherins is mediated by dimerization of their EC1 domains through the 'swapping' of N-terminal β-strands. We use molecular simulations, measurements of binding affinities and X-ray crystallography to provide a detailed picture of the structural and energetic factors that control the adhesive dimerization of cadherins. We show that strand swapping in EC1 is driven by conformational strain in cadherin monomers that arises from the anchoring of their short N-terminal strand at one end by the conserved Trp2 and at the other by ligation to Ca(2+) ions. We also demonstrate that a conserved proline-proline motif functions to avoid the formation of an overly tight interface where affinity differences between different cadherins, crucial at the cellular level, are lost. We use these findings to design site-directed mutations that transform a monomeric EC2-EC3 domain cadherin construct into a strand-swapped dimer.

Indexed as

Protein MultimerizationAmino Acid SequenceAnimalsCadherinsCalciumCations, DivalentCrystallography, X-RayMiceModels, ChemicalModels, MolecularMolecular Dynamics SimulationMolecular Sequence DataMutagenesis, Site-DirectedMutant ProteinsProtein BindingProtein ConformationCadherinsCalciumCations, DivalentMutant Proteins

Identifiers

PMID21572446
PMCPMC3113550
OpenAlexW2065884849

What OpenQuestion holds

Textmetadata
LicenceTDM
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.