Evidence map›Paper›PMID 12672958›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2003

Solution structure of a functionally active fragment of decay-accelerating factor.

Stanislava Uhrinova, Feng Lin, Graeme Ball, Krystyna Bromek, Dusan Uhrin, M Edward Medof, Paul N Barlow

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

15 citing papers in PubMed, 47 citations in OpenAlex.

  1. Molecular engineering of an efficient four-domain DAF-MCP chimera reveals the presence of functional modularity in RCA proteins.Proceedings of the National Academy of Sciences of the United States of America · 2019
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  9. The structure of C2b, a fragment of complement component C2 produced during C3 convertase formation.Acta crystallographica. Section D, Biological crystallography · 2009
    Article
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  13. Structure of vaccinia complement protein in complex with heparin and potential implications for complement regulation.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Article
  14. Article
  15. Complement regulation at the molecular level: the structure of decay-accelerating factor.Proceedings of the National Academy of Sciences of the United States of America · 2004
    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

7 authors at 1 institution in 1 country.

Stanislava UhrinovaEdinburgh Protein Interaction Centre, University of Edinburgh, Edinburgh EH9 3JJ, Scotland.
Feng Lin
Graeme Ball
Krystyna Bromek
Dusan Uhrin
M Edward Medof
Paul N Barlow
Case Western Reserve University · US

Funding

ROLE OF DAF IN THE COMPLEMENT CASCADE ND IN PNHR01AI023598 · NIAID · CASE WESTERN RESERVE UNIVERSITY · PI MEDOF, MELVIN EDWARD · 1985 to 2009
$3.8M
NIAID NIH HHS AI 23598NIAID NIH HHS R01 AI023598
6 · The paper itself

Abstract

The second and third modules of human decay accelerating factor (DAF) are necessary and sufficient to accelerate decay of the classical pathway (CP) convertase of complement. No structure of a mammalian protein with decay-accelerating activity has been available to date. We therefore determined the solution structure of DAF modules 2 and 3 (DAF approximately 2,3). Structure-guided analysis of 24 mutants identified likely contact points between DAF and the CP convertase. Three (R96, R69, and a residue in the vicinity of L171) lie on DAF approximately 2,3's concave face. A fourth, consisting of K127 and nearby R100, is on the opposite face. Regions of module 3 remote from the semiflexible 2-3 interface seem not to be involved in binding to the CP convertase. DAF thus seems to occupy a groove on the CP convertase such that both faces of DAF close to the 2-3 junction (including a positively charged region that encircles the protein at this point) interact simultaneously. Alternative pathway convertase interactions with DAF require additional regions of CCP 3 lying away from the 2-3 interface, consistent with the established additional requirement of module 4 for alternative pathway regulation.

Indexed as

Binding SitesCD55 AntigensComplement C3-C5 ConvertasesHumansModels, MolecularMutagenesis, Site-DirectedNuclear Magnetic Resonance, BiomolecularPeptide FragmentsProtein ConformationRecombinant ProteinsSolutionsStatic ElectricityThermodynamicsCD55 AntigensComplement C3-C5 ConvertasesPeptide FragmentsRecombinant ProteinsSolutions

Identifiers

PMID12672958
PMCPMC153622
OpenAlexW2087978053

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.