Evidence map›Paper›PMID 24316400›Full record

ArticleStructure (London, England : 1993)2014

Structure and self-assembly of the calcium binding matrix protein of human metapneumovirus.

Cedric Leyrat, Max Renner, Karl Harlos, Juha T Huiskonen, Jonathan M Grimes

Open access · hybridAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
3.5field-weighted citation impact, top 7% 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, 58 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Cedric LeyratDivision of Structural Biology, The Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, UK.
Max RennerDivision of Structural Biology, The Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, UK.
Karl HarlosDivision of Structural Biology, The Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, UK.
Juha T HuiskonenDivision of Structural Biology, The Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, UK.
Jonathan M GrimesDivision of Structural Biology, The Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, UK; Diamond Light Source Limited, Harwell Science and Innovation Campus, Didcot, Oxfordshire, OX11 0DE, UK. Electronic address: jonathan@strubi.ox.ac.uk.
University of Oxford · GBCentre for Human Genetics · GB

Funding

Wellcome Trust 060208/Z/00/ZWellcome Trust 090532Wellcome Trust 090532/Z/09/ZWellcome Trust 093305/Z/10/Z
6 · The paper itself

Abstract

The matrix protein (M) of paramyxoviruses plays a key role in determining virion morphology by directing viral assembly and budding. Here, we report the crystal structure of the human metapneumovirus M at 2.8 Å resolution in its native dimeric state. The structure reveals the presence of a high-affinity Ca²⁺ binding site. Molecular dynamics simulations (MDS) predict a secondary lower-affinity site that correlates well with data from fluorescence-based thermal shift assays. By combining small-angle X-ray scattering with MDS and ensemble analysis, we captured the structure and dynamics of M in solution. Our analysis reveals a large positively charged patch on the protein surface that is involved in membrane interaction. Structural analysis of DOPC-induced polymerization of M into helical filaments using electron microscopy leads to a model of M self-assembly. The conservation of the Ca²⁺ binding sites suggests a role for calcium in the replication and morphogenesis of pneumoviruses.

Indexed as

CalciumCalcium-Binding ProteinsEscherichia coliHumansMetapneumovirusMicroscopy, ElectronMolecular Dynamics SimulationPhosphatidylcholinesProtein MultimerizationProtein Structure, SecondaryProtein Structure, TertiaryRecombinant ProteinsScattering, Small AngleThermodynamicsViral Matrix ProteinsVirion1,2-oleoylphosphatidylcholineCalciumCalcium-Binding ProteinsPhosphatidylcholinesRecombinant ProteinsViral Matrix Proteins

Identifiers

PMID24316400
PMCPMC3887258
OpenAlexW2005209853

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.