Evidence map›Paper›PMID 26384592›Full record

ArticleProtein science : a publication of the Protein Society2015

Structural insights into the intertwined dimer of fyn SH2.

Radu Huculeci, Abel Garcia-Pino, Lieven Buts, Tom Lenaerts, Nico van Nuland

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.6field-weighted citation impact, top 30% 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

5 citing papers in PubMed, 7 citations in OpenAlex.

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  5. Selection on protein structure, interaction, and sequence.Protein science : a publication of the Protein Society · 2016
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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

5 authors at 3 institutions in 1 country.

Radu HuculeciStructural Biology Brussels, Jean Jeener NMR Center, Vrije Universiteit Brussel, Brussels, Belgium.
Abel Garcia-PinoStructural Biology Brussels, Jean Jeener NMR Center, Vrije Universiteit Brussel, Brussels, Belgium.
Lieven ButsStructural Biology Brussels, Jean Jeener NMR Center, Vrije Universiteit Brussel, Brussels, Belgium.
Tom LenaertsMLG, Département d'Informatique, Université Libre de Bruxelles, Brussels, Belgium.
Nico van NulandStructural Biology Brussels, Jean Jeener NMR Center, Vrije Universiteit Brussel, Brussels, Belgium.
VIB-VUB Center for Structural Biology · BEVrije Universiteit Brussel · BEUniversité Libre de Bruxelles · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Src homology 2 domains are interaction modules dedicated to the recognition of phosphotyrosine sites incorporated in numerous proteins found in intracellular signaling pathways. Here we provide for the first time structural insight into the dimerization of Fyn SH2 both in solution and in crystalline conditions, providing novel crystal structures of both the dimer and peptide-bound structures of Fyn SH2. Using nuclear magnetic resonance chemical shift analysis, we show how the peptide is able to eradicate the dimerization, leading to monomeric SH2 in its bound state. Furthermore, we show that Fyn SH2's dimer form differs from other SH2 dimers reported earlier. Interestingly, the Fyn dimer can be used to construct a completed dimer model of Fyn without any steric clashes. Together these results extend our understanding of SH2 dimerization, giving structural details, on one hand, and suggesting a possible physiological relevance of such behavior, on the other hand.

Indexed as

Crystallography, X-RayHumansModels, MolecularPeptidesPhosphotyrosineProtein MultimerizationProtein Structure, SecondaryProto-Oncogene Proteins c-fynsrc Homology DomainsFYN protein, humanPeptidesPhosphotyrosineProto-Oncogene Proteins c-fyncrystal structuresFynhomodimerNMR analysisSH2

Identifiers

PMID26384592
PMCPMC4815226
OpenAlexW2163161477

What OpenQuestion holds

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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.