Evidence map›Paper›PMID 26146185›Full record

ArticleStructure (London, England : 1993)2015

Structures of CD6 and Its Ligand CD166 Give Insight into Their Interaction.

Paul E Chappell, Lee I Garner, Jun Yan, Clive Metcalfe, Deborah Hatherley, Steven Johnson, Carol V Robinson, Susan M Lea, Marion H Brown

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed, 1 pooled it
4.0field-weighted citation impact, top 5% 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

46 citing papers in PubMed, 1 synthesis or guideline pooled it, 71 citations in OpenAlex.

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  18. 3D Structures of IgA, IgM, and Components.International journal of molecular sciences · 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

9 authors at 1 institution in 1 country.

Paul E ChappellSir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.
Lee I GarnerSir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.
Jun YanDepartment of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.
Clive MetcalfeSir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.
Deborah HatherleySir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.
Steven JohnsonSir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.
Carol V RobinsonDepartment of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.
Susan M LeaSir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.
Marion H BrownSir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK. Electronic address: marion.brown@path.ox.ac.uk.
University of Oxford · GB

Funding

Biotechnology and Biological Sciences Research Council BB/F016085/1Medical Research Council G0400808Medical Research Council MR/M011984/1Wellcome Trust 100298Wellcome Trust 100298/Z/12/Z
6 · The paper itself

Abstract

CD6 is a transmembrane protein with an extracellular region containing three scavenger receptor cysteine rich (SRCR) domains. The membrane proximal domain of CD6 binds the N-terminal immunoglobulin superfamily (IgSF) domain of another cell surface receptor, CD166, which also engages in homophilic interactions. CD6 expression is mainly restricted to T cells, and the interaction between CD6 and CD166 regulates T-cell activation. We have solved the X-ray crystal structures of the three SRCR domains of CD6 and two N-terminal domains of CD166. This first structure of consecutive SRCR domains reveals a nonlinear organization. We characterized the binding sites on CD6 and CD166 and showed that a SNP in CD6 causes glycosylation that hinders the CD6/CD166 interaction. Native mass spectrometry analysis showed that there is competition between the heterophilic and homophilic interactions. These data give insight into how interactions of consecutive SRCR domains are perturbed by SNPs and potential therapeutic reagents.

Indexed as

Models, MolecularPolymorphism, Single NucleotideActivated-Leukocyte Cell Adhesion MoleculeAmino Acid MotifsAnimalsAntigens, CDAntigens, Differentiation, T-LymphocyteBinding SitesCell Adhesion Molecules, NeuronalCHO CellsCloning, MolecularCricetulusCrystallography, X-RayEscherichia coliFetal ProteinsGene ExpressionActivated-Leukocyte Cell Adhesion MoleculeALCAM protein, humanAntigens, CDAntigens, Differentiation, T-LymphocyteCD6 antigenCell Adhesion Molecules, NeuronalFetal ProteinsRecombinant Fusion Proteins

Identifiers

PMID26146185
PMCPMC4533223
OpenAlexW1649473267

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.