Evidence map›Paper›PMID 15795319›Full record

ArticleThe Journal of cell biology2005

Three-dimensional EM structure of the ectodomain of integrin {alpha}V{beta}3 in a complex with fibronectin.

Brian D Adair, Jian-Ping Xiong, Catherine Maddock, Simon L Goodman, M Amin Arnaout, Mark Yeager

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed
8.6field-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

90 citing papers in PubMed, 184 citations in OpenAlex.

  1. Integrins as key regulators in tumor perineural invasion: mechanisms and clinical implications.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2026
    Review
  2. Review
  3. Article
  4. Article
  5. Human Saposin B Ligand Binding and Presentation to α-Galactosidase A.bioRxiv : the preprint server for biology · 2024
    Article
  6. Article
  7. Targeting integrin pathways: mechanisms and advances in therapy.Signal transduction and targeted therapy · 2023
    Review
  8. Review
  9. Review
  10. Review
  11. β2 integrin activation and signal transduction in leukocyte recruitment.American journal of physiology. Cell physiology · 2021
    Review
  12. Review
  13. Roles of Membrane Domains in Integrin-Mediated Cell Adhesion.International journal of molecular sciences · 2020
    Review
  14. Unique transmembrane domain interactions differentially modulate integrin αvβ3 and αIIbβ3 function.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  15. Article
  16. Review
  17. Review
  18. Activation mechanisms of αVβ3 integrin by binding to fibronectin: A computational study.Protein science : a publication of the Protein Society · 2017
    Article
  19. Article
  20. The role of integrins in glaucoma.Experimental eye research · 2017
    Review

30 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

6 authors at 4 institutions in 2 countries.

Brian D AdairDepartment of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Jian-Ping Xiong
Catherine Maddock
Simon L Goodman
M Amin Arnaout
Mark Yeager
Massachusetts General Hospital · USMerck (Germany) · DEScripps Clinic · USScripps Research Institute · US

Funding

Structure and Function of beta2 IntegrinR01DK048549 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI ARNAOUT, M. AMIN · 1994 to 2016
$6.0M
MOLECULAR BASIS OF VIRAL PATHOGENESIST32AI007354 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI DE LA TORRE, JUAN C. · 1989 to 2020
$5.2M
NIAID NIH HHS AI-07354NIAID NIH HHS T32 AI007354NIDDK NIH HHS R01 DK048549
6 · The paper itself

Abstract

Integrins are alphabeta heterodimeric cell surface receptors that mediate transmembrane signaling by binding extracellular and cytoplasmic ligands. The ectodomain of integrin alphaVbeta3 crystallizes in a bent, genuflexed conformation considered to be inactive (unable to bind physiological ligands in solution) unless it is fully extended by activating stimuli. We generated a stable, soluble complex of the Mn(2+)-bound alphaVbeta3 ectodomain with a fragment of fibronectin (FN) containing type III domains 7 to 10 and the EDB domain (FN7-EDB-10). Transmission electron microscopy and single particle image analysis were used to determine the three-dimensional structure of this complex. Most alphaVbeta3 particles, whether unliganded or FN-bound, displayed compact, triangular shapes. A difference map comparing ligand-free and FN-bound alphaVbeta3 revealed density that could accommodate the RGD-containing FN10 in proximity to the ligand-binding site of beta3, with FN9 just adjacent to the synergy site binding region of alphaV. We conclude that the ectodomain of alphaVbeta3 manifests a bent conformation that is capable of stably binding a physiological ligand in solution.

Indexed as

Binding SitesCell MembraneFibronectinsHumansImaging, Three-DimensionalIntegrin alphaVbeta3LigandsMacromolecular SubstancesMicroscopy, Electron, TransmissionProtein BindingProtein Structure, QuaternaryProtein Structure, TertiaryFibronectinsIntegrin alphaVbeta3LigandsMacromolecular Substances

Identifiers

PMID15795319
PMCPMC2171847
OpenAlexW2114213585

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.