Evidence map›Paper›PMID 28132784›Full record

ArticleStructure (London, England : 1993)2017

Crystal Structure of the Heterotrimeric Integrin-Binding Region of Laminin-111.

David Pulido, Sadaf-Ahmahni Hussain, Erhard Hohenester

Open access · hybridAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

19 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Chapter 22: Structural and signaling functions of integrins.Biochimica et biophysica acta. Biomembranes · 2020
    Review
  11. Article
  12. Structural biology of laminins.Essays in biochemistry · 2019
    Review
  13. Article
  14. Laminin G-like domains: dystroglycan-specific lectins.Current opinion in structural biology · 2019
    Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. 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

3 authors at 1 institution in 1 country.

David PulidoDepartment of Life Sciences, Imperial College London, Sir Ernst Chain Building, London SW7 2AZ, UK.
Sadaf-Ahmahni HussainDepartment of Life Sciences, Imperial College London, Sir Ernst Chain Building, London SW7 2AZ, UK.
Erhard HohenesterDepartment of Life Sciences, Imperial College London, Sir Ernst Chain Building, London SW7 2AZ, UK. Electronic address: e.hohenester@imperial.ac.uk.
Imperial College London · GB

Funding

Wellcome TrustWellcome Trust 101748/Z/13/Z
6 · The paper itself

Abstract

Laminins are cell-adhesive glycoproteins that are essential for basement membrane assembly and function. Integrins are important laminin receptors, but their binding site on the heterotrimeric laminins is poorly defined structurally. We report the crystal structure at 2.13 Å resolution of a minimal integrin-binding fragment of mouse laminin-111, consisting of ∼50 residues of α1β1γ1 coiled coil and the first three laminin G-like (LG) domains of the α1 chain. The LG domains adopt a triangular arrangement, with the C terminus of the coiled coil situated between LG1 and LG2. The critical integrin-binding glutamic acid residue in the γ1 chain tail is surface exposed and predicted to bind to the metal ion-dependent adhesion site in the integrin β1 subunit. Additional contacts to the integrin are likely to be made by the LG1 and LG2 surfaces adjacent to the γ1 chain tail, which are notably conserved and free of obstructing glycans.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCell AdhesionCell LineConserved SequenceCrystallography, X-RayHumansIntegrinsLamininMiceModels, MolecularProtein BindingProtein Structure, QuaternaryProtein Structure, SecondaryIntegrinsLaminincell adhesioncoiled coilextracellular matrixintegrinlaminin

Identifiers

PMID28132784
PMCPMC5343747
OpenAlexW2581624131

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.