Evidence map›Paper›PMID 16328780›Full record

ArticleJournal of biomedical science2006

Solution structure of the X4 protein coded by the SARS related coronavirus reveals an immunoglobulin like fold and suggests a binding activity to integrin I domains.

Karen Hänel, Thomas Stangler, Matthias Stoldt, Dieter Willbold

Abstract read
In one paragraph

Article in Journal of biomedical science, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

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  11. Characterization of the SARS-CoV-2 coronavirus X4-like accessory protein.The Egyptian journal of medical human genetics · 2021
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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.

Karen HänelForschungszentrum Jülich, Institut für Biologische Informationsverarbeitung (IBI-2), Germany.
Thomas Stangler
Matthias Stoldt
Dieter Willbold

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The SARS related Coronavirus genome contains a variety of novel accessory genes. One of these, called ORF7a or ORF8, code for a protein, known as 7a, U122 or X4. We set out to determine the three-dimensional structure of the soluble ectodomain of this type-I transmembrane protein by nuclear magnetic resonance spectroscopy. The fold of the protein is the first member of a further variation of the immunoglobulin like beta-sandwich fold. Because X4 does not reveal significant sequence homologies to proteins in the data bases, we carried out a structure based similarity search for proteins with known function. High structural similarity to Dl domains of ICAM-1 and ICAM-2, and common features in amino acid sequence between X4 and ICAM-1, suggest X4 to possess binding activity for the alpha(L) integrin I domain of LFA-1. Further, based on this structure based prediction, potential functions of X4 in virus replication and pathogenesis are discussed.

Indexed as

Amino Acid SequenceAntigens, CDCell Adhesion MoleculesCloning, MolecularHumansImmunoglobulinsIntegrinsIntercellular Adhesion Molecule-1Interleukin-1Lymphocyte Function-Associated Antigen-1Models, MolecularMolecular Sequence DataOpen Reading FramesProtein Structure, SecondaryProtein Structure, TertiarySevere acute respiratory syndrome-related coronavirusAntigens, CDCell Adhesion MoleculesICAM2 protein, humanImmunoglobulinsIntegrinsIntercellular Adhesion Molecule-1Interleukin-1Lymphocyte Function-Associated Antigen-1sars7a protein, SARS virusViral Matrix ProteinsViral Proteins

Identifiers

PMID16328780
PMCPMC7089389

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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.