Evidence map›Paper›PMID 25168678›Full record

ArticleEMBO reports2014

The crystal structure of the phosphatidylinositol 4-kinase IIα.

Adriana Baumlova, Dominika Chalupska, Bartosz Róźycki, Marko Jovic, Eva Wisniewski, Martin Klima, Anna Dubankova, Daniel P Kloer, Radim Nencka, Tamas Balla and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in EMBO reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

25 citing papers in PubMed, 62 citations in OpenAlex.

  1. Review
  2. Phosphatidylinositol 4-phosphate; A minor lipid with multiple personalities.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2025
    Review
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  20. T4 lysozyme-facilitated crystallization of the human molybdenum cofactor-dependent enzyme mARC.Acta crystallographica. Section F, Structural biology communications · 2018
    Article
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

11 authors at 4 institutions in 4 countries.

Adriana BaumlovaInstitute of Organic Chemistry and Biochemistry AS CR, Prague, Czech Republic.
Dominika ChalupskaInstitute of Organic Chemistry and Biochemistry AS CR, Prague, Czech Republic.
Bartosz RóźyckiInstitute of Physics Polish Academy of Sciences, Warsaw, Poland.
Marko JovicSection on Molecular Signal Transduction, Program for Developmental Neuroscience, NICHD NIH, Bethesda, MD, USA.
Eva WisniewskiSection on Molecular Signal Transduction, Program for Developmental Neuroscience, NICHD NIH, Bethesda, MD, USA.
Martin KlimaInstitute of Organic Chemistry and Biochemistry AS CR, Prague, Czech Republic.
Anna DubankovaInstitute of Organic Chemistry and Biochemistry AS CR, Prague, Czech Republic.
Daniel P KloerSyngenta Jealott's Hill Internation Research Centre, Bracknell, UK.
Radim NenckaInstitute of Organic Chemistry and Biochemistry AS CR, Prague, Czech Republic.
Tamas BallaSection on Molecular Signal Transduction, Program for Developmental Neuroscience, NICHD NIH, Bethesda, MD, USA.
Evzen BouraInstitute of Organic Chemistry and Biochemistry AS CR, Prague, Czech Republic boura@uochb.cas.cz.
Czech Academy of Sciences, Institute of Organic Chemistry and Biochemistry · CZEunice Kennedy Shriver National Institute of Child Health and Human Development · USInstitute of Physics · PLSyngenta (United Kingdom) · GB

Funding

Phosphoinositide-calcium Signaling In Cell RegulationZIAHD000196 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI BALLA, TAMAS · 2009 to 2025
$26.3M
6 · The paper itself

Abstract

Phosphoinositides are a class of phospholipids generated by the action of phosphoinositide kinases with key regulatory functions in eukaryotic cells. Here, we present the atomic structure of phosphatidylinositol 4-kinase type IIα (PI4K IIα), in complex with ATP solved by X-ray crystallography at 2.8 Å resolution. The structure revealed a non-typical kinase fold that could be divided into N- and C-lobes with the ATP binding groove located in between. Surprisingly, a second ATP was found in a lateral hydrophobic pocket of the C-lobe. Molecular simulations and mutagenesis analysis revealed the membrane binding mode and the putative function of the hydrophobic pocket. Taken together, our results suggest a mechanism of PI4K IIα recruitment, regulation, and function at the membrane.

Indexed as

Crystallography, X-RayProtein ConformationBinding SitesHumansInositolMembranesMinor Histocompatibility AntigensMonte Carlo MethodPhosphatidylinositolsPhosphotransferases (Alcohol Group Acceptor)Protein BindingSignal TransductionInositolMinor Histocompatibility Antigensphosphatidylinositol phosphate 4-kinasePhosphatidylinositolsPhosphotransferases (Alcohol Group Acceptor)crystal structurekinasemembraneMonte Carlo simulationsphosphatidyl inositol

Identifiers

PMID25168678
PMCPMC4253849
OpenAlexW2039885017

What OpenQuestion holds

Textmetadata
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.