Evidence map›Paper›PMID 15079089›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2004

Crystal structure of the von Willebrand factor A domain of human capillary morphogenesis protein 2: an anthrax toxin receptor.

D Borden Lacy, Darran J Wigelsworth, Heather M Scobie, John A T Young, R John Collier

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
–field-weighted citation impact
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

65 citing papers in PubMed.

  1. Article
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  12. CaComputational and structural biotechnology journal · 2020
    Article
  13. Article
  14. A three-way inter-molecular network accounts for the CaThe Journal of biological chemistry · 2018
    Article
  15. Cell adhesion molecule control of planar spindle orientation.Cellular and molecular life sciences : CMLS · 2016
    Review
  16. Review
  17. Review
  18. Anti-infective immunoadhesins from plants.Plant biotechnology journal · 2015
    Review
  19. Article
  20. Article

5 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

5 authors.

D Borden LacyDepartment of Microbiology and Molecular Genetics, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA.
Darran J Wigelsworth
Heather M Scobie
John A T Young
R John Collier

Funding

Multivalent display of anthrax toxin inhibitorsP01AI056013 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI MANCHESTER, MARIANNE · 2003 to 2007
$9.2M
MOLECULAR MECHANISMS OF BACTERIAL PATHOGENESISR37AI022021 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI COLLIER, ROBERT JOHN · 1988 to 2007
$6.1M
STRATEGIES TO INHIBIT CELLULAR UPTAKE OF ANTHRAX TOXINR01AI048489 · NIAID · UNIVERSITY OF WISCONSIN MADISON · PI YOUNG, JOHN A T · 2000 to 2008
$4.4M
MOLECULAR MECHANISMS OF BACTERIAL PATHOGENESISR01AI022021 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI COLLIER, ROBERT JOHN · 1985 to 2012
$3.9M
NIAID NIH HHS AI022021NIAID NIH HHS AI048489NIAID NIH HHS AI056013NIAID NIH HHS P01 AI056013NIAID NIH HHS R01 AI022021NIAID NIH HHS R01 AI048489NIAID NIH HHS R37 AI022021
6 · The paper itself

Abstract

Anthrax toxin is released from Bacillus anthracis as three monomeric proteins, which assemble into toxic complexes at the surface of receptor-bearing host cells. One of the proteins, protective antigen (PA), binds to receptors and orchestrates the delivery of the other two (the lethal and edema factors) into the cytosol. PA has been shown to bind to two cellular receptors: anthrax toxin receptor/tumor endothelial marker 8 and capillary morphogenesis protein 2 (CMG2). Both are type 1 membrane proteins that include an approximately 200-aa extracellular von Willebrand factor A (VWA) domain with a metal ion-dependent adhesion site (MIDAS) motif. The anthrax toxin receptor/tumor endothelial marker 8 and CMG2 VWA domains share approximately 60% amino acid identity and bind PA directly in a metal-dependent manner. Here, we report the crystal structure of the CMG2 VWA domain, with and without its intramolecular disulfide bond, to 1.5 and 1.8 A, respectively. Both structures contain a carboxylate ligand-mimetic bound at the MIDAS and appear as open conformations when compared with the VWA domains from alpha-integrins. The CMG2 structures provide a template to begin probing the high-affinity CMG2-PA interaction (200 pM) and may facilitate understanding of toxin assembly/internalization and the development of new anthrax treatments. The structural data also allow molecular interpretation of known CMG2 VWA domain mutations linked to the genetic disorders, juvenile hyaline fibromatosis, and infantile systemic hyalinosis.

Indexed as

Amino Acid SequenceCrystallography, X-RayHumansMembrane ProteinsModels, MolecularMolecular Sequence DataProtein ConformationReceptors, PeptideSequence Homology, Amino Acidvon Willebrand Factoranthrax toxin receptorsANTXR2 protein, humanMembrane ProteinsReceptors, Peptidevon Willebrand Factor

Identifiers

PMID15079089
PMCPMC404051

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.