Evidence map›Paper›PMID 24187131›Full record

ArticleThe Journal of biological chemistry2013

The structure of integrin α1I domain in complex with a collagen-mimetic peptide.

Yanni K-Y Chin, Stephen J Headey, Biswaranjan Mohanty, Rahul Patil, Paul A McEwan, James D Swarbrick, Terrence D Mulhern, Jonas Emsley, Jamie S Simpson, Martin J Scanlon

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
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  5. Review
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  10. Unique charge-dependent constraint on collagen recognition by integrin α10β1.Matrix biology : journal of the International Society for Matrix Biology · 2017
    Article
  11. Article
  12. Article
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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

10 authors.

Yanni K-Y ChinFrom Medicinal Chemistry, Monash Institute of Pharmaceutical Sciences and.
Stephen J Headey
Biswaranjan Mohanty
Rahul Patil
Paul A McEwan
James D Swarbrick
Terrence D Mulhern
Jonas Emsley
Jamie S Simpson
Martin J Scanlon

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have determined the structure of the human integrin α1I domain bound to a triple-helical collagen peptide. The structure of the α1I-peptide complex was investigated using data from NMR, small angle x-ray scattering, and size exclusion chromatography that were used to generate and validate a model of the complex using the data-driven docking program, HADDOCK (High Ambiguity Driven Biomolecular Docking). The structure revealed that the α1I domain undergoes a major conformational change upon binding of the collagen peptide. This involves a large movement in the C-terminal helix of the αI domain that has been suggested to be the mechanism by which signals are propagated in the intact integrin receptor. The structure suggests a basis for the different binding selectivity observed for the α1I and α2I domains. Mutational data identify residues that contribute to the conformational change observed. Furthermore, small angle x-ray scattering data suggest that at low collagen peptide concentrations the complex exists in equilibrium between a 1:1 and 2:1 α1I-peptide complex.

Indexed as

Biomimetic MaterialsCollagenHumansIntegrin alpha1Molecular Docking SimulationPeptidesProtein BindingProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, TertiaryScattering, Small AngleX-Ray DiffractionCollagenIntegrin alpha1PeptidesCollagenExtracellular MatrixIntegrinsNMRProtein-Protein InteractionsProtein Structure

Identifiers

PMID24187131
PMCPMC3873540

What OpenQuestion holds

Textmetadata
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Registered trials

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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.