Evidence map›Paper›PMID 19553699›Full record

ArticleThe Journal of biological chemistry2009

Crystal structure of the LG1-3 region of the laminin alpha2 chain.

Federico Carafoli, Naomi J Clout, Erhard Hohenester

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

18 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. Evidence of Two NovelFrontiers in neurology · 2022
    Article
  4. Article
  5. Structural modeling, mutation analysis, andComputational and structural biotechnology journal · 2020
    Article
  6. Structural biology of laminins.Essays in biochemistry · 2019
    Review
  7. Review
  8. Article
  9. Article
  10. Cross-linking reveals laminin coiled-coil architecture.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. Review
  17. The laminin family.Cell adhesion & migration
    Review
  18. Review
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.

Federico CarafoliDepartment of Life Sciences, Imperial College London, London SW7 2AZ, United Kingdom.
Naomi J Clout
Erhard Hohenester
Imperial College London · GB

Funding

Biotechnology and Biological Sciences Research Council BB/D524840/1Biotechnology and Biological Sciences Research Council BBD5248401Wellcome Trust 054334Wellcome Trust 083942
6 · The paper itself

Abstract

Laminins are large heterotrimeric glycoproteins with many essential functions in basement membrane assembly and function. Cell adhesion to laminins is mediated by a tandem of five laminin G-like (LG) domains at the C terminus of the alpha chain. Integrin binding requires an intact LG1-3 region, as well as contributions from the coiled coil formed by the alpha, beta, and gamma chains. We have determined the crystal structure at 2.8-A resolution of the LG1-3 region of the laminin alpha2 chain (alpha 2LG1-3). The three LG domains adopt typical beta-sandwich folds, with canonical calcium binding sites in LG1 and LG2. LG2 and LG3 interact through a substantial interface, but LG1 is completely dissociated from the LG2-3 pair. We suggest that the missing gamma chain tail may be required to stabilize the interaction between LG1 and LG2-3 in the biologically active conformation. A global analysis of N-linked glycosylation sites shows that the beta-sandwich faces of LG1 are free of carbohydrate modifications in all five laminin alpha chains, suggesting that these surfaces may harbor the integrin binding site. The alpha 2LG1-3 structure provides the first atomic view of the integrin binding region of laminins.

Indexed as

Models, MolecularAmino Acid SequenceCell LineHumansLamininMolecular Sequence DataProtein Structure, SecondaryProtein Structure, TertiarySequence Homology, Amino AcidLamininlaminin alpha 2

Identifiers

PMID19553699
PMCPMC2755686
OpenAlexW2031964906

What OpenQuestion holds

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LicenceCC BY-NC
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.