Evidence map›Paper›PMID 12970173›Full record

ArticleThe EMBO journal2003

Structure of integrin alpha5beta1 in complex with fibronectin.

Junichi Takagi, Konstantin Strokovich, Timothy A Springer, Thomas Walz

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 154 papers.

0numbers the graph read from it
0cells of the map it votes in
154citing papers in PubMed
8.9field-weighted citation impact, top 1% 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

154 citing papers in PubMed, 340 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Article
  5. MnBiophysical journal · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Conformational response of αStructure (London, England : 1993) · 2025
    Article
  10. Article
  11. Review
  12. Article
  13. Contributions of the individual domains of αCytoskeleton (Hoboken, N.J.) · 2024
    Article
  14. Multiscale models of integrins and cellular adhesions.Current opinion in structural biology · 2023
    Review
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Review

94 more citing papers are in PubMed but not listed here.

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

4 authors at 1 institution in 2 countries.

Junichi TakagiThe Center for Blood Research, Department of Pediatrics, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA. takagi@protein.osaka-u.ac.jp
Konstantin Strokovich
Timothy A Springer
Thomas Walz
Protein Research Foundation · JP

Funding

Single particle reconstructionP01GM062580 · NIGMS · HARVARD MEDICAL SCHOOL · PI WALZ, THOMAS · 2001 to 2016
$23.7M
STRUCTURE OF INTEGRINS AND YWTD BETA PROPELLER DOMAINSP01HL048675 · NHLBI · IMMUNE DISEASE INSTITUTE, INC. · PI SPRINGER, TIMOTHY A · 1992 to 2009
$20.9M
NHLBI NIH HHS HL48675NHLBI NIH HHS P01 HL048675NIGMS NIH HHS GM62580NIGMS NIH HHS P01 GM062580
6 · The paper itself

Abstract

The membrane-distal headpiece of integrins has evolved to specifically bind large extracellular protein ligands, but the molecular architecture of the resulting complexes has not been determined. We used molecular electron microscopy to determine the three-dimensional structure of the ligand-binding headpiece of integrin alpha5beta1 complexed with fragments of its physiological ligand fibronectin. The density map for the unliganded alpha5beta1 headpiece shows a 'closed' conformation similar to that seen in the alphaVbeta3 crystal structure. By contrast, binding to fibronectin induces an 'open' conformation with a dramatic, approximately 80 degrees change in the angle of the hybrid domain of the beta subunit relative to its I-like domain. The fibronectin fragment binds to the interface between the beta-propeller and I-like domains in the integrin headpiece through the RGD-containing module 10, but direct contact of the synergy-region-containing module 9 to integrin is not evident. This finding is corroborated by kinetic analysis of real-time binding data, which shows that the synergy site greatly enhances k(on) but has little effect on the stability or k(off) of the complex.

Indexed as

Amino Acid SubstitutionCrystallography, X-RayFibronectinsHumansIntegrin alpha5beta1KineticsLigandsProtein BindingProtein ConformationRecombinant ProteinsFibronectinsIntegrin alpha5beta1LigandsRecombinant Proteins

Identifiers

PMID12970173
PMCPMC212714
OpenAlexW1973800056

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.