Evidence map›Paper›PMID 27974389›Full record

ArticleThe Biochemical journal2017

Structure and lipid-binding properties of the kindlin-3 pleckstrin homology domain.

Tao Ni, Antreas C Kalli, Fiona B Naughton, Luke A Yates, Omar Naneh, Mirijam Kozorog, Gregor Anderluh, Mark S P Sansom, Robert J C Gilbert

Open access · hybridAbstract read
In one paragraph

Article in The Biochemical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

33 citing papers in PubMed, 51 citations in OpenAlex.

  1. Phospholipases: Where Do We Stand?Methods in molecular biology (Clifton, N.J.) · 2027
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  10. Radiotherapy enhances CXCR3Cancer immunology, immunotherapy : CII · 2023
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  18. Article
  19. Article
  20. β2 integrin activation and signal transduction in leukocyte recruitment.American journal of physiology. Cell physiology · 2021
    Review
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 2 institutions in 2 countries.

Tao NiDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, U.K.
Antreas C KalliDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, U.K.
Fiona B NaughtonDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, U.K.
Luke A YatesDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, U.K.
Omar NanehDepartment for Molecular Biology and Nanobiotechnology, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia.
Mirijam KozorogDepartment for Molecular Biology and Nanobiotechnology, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia.
Gregor AnderluhDepartment for Molecular Biology and Nanobiotechnology, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia.
Mark S P SansomDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, U.K. mark.sansom@bioch.ox.ac.uk gilbert@strubi.ox.ac.uk.
Robert J C GilbertDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, U.K. mark.sansom@bioch.ox.ac.uk gilbert@strubi.ox.ac.uk.
National Institute of Chemistry · SIUniversity of Oxford · GB

Funding

British Heart Foundation PG/14/8/30627Wellcome Trust 060208/Z/00/ZWellcome Trust 090532/Z/09/ZWellcome Trust 093305/Z/10/ZWellcome Trust WT092970MA
6 · The paper itself

Abstract

Kindlins co-activate integrins alongside talin. They possess, like talin, a FERM domain (4.1-erythrin-radixin-moiesin domain) comprising F0-F3 subdomains, but with a pleckstrin homology (PH) domain inserted in the F2 subdomain that enables membrane association. We present the crystal structure of murine kindlin-3 PH domain determined at a resolution of 2.23 Å and characterise its lipid binding using biophysical and computational approaches. Molecular dynamics simulations suggest flexibility in the PH domain loops connecting β-strands forming the putative phosphatidylinositol phosphate (PtdInsP)-binding site. Simulations with PtdInsP-containing bilayers reveal that the PH domain associates with PtdInsP molecules mainly via the positively charged surface presented by the β1-β2 loop and that it binds with somewhat higher affinity to PtdIns(3,4,5)P

Indexed as

Pleckstrin Homology DomainsAmino Acid SequenceAnimalsBinding SitesCloning, MolecularCrystallography, X-RayCytoskeletal ProteinsEscherichia coliGene ExpressionKineticsMiceMolecular Dynamics SimulationPhosphatidylcholinesPhosphatidylinositolsPhosphatidylserinesProtein Binding1-palmitoyl-2-oleoylglycero-3-phosphoserine1-palmitoyl-2-oleoylphosphatidylcholineCytoskeletal Proteinskindlin-3 protein, mousePhosphatidylcholinesphosphatidylinositol receptorsPhosphatidylinositolsPhosphatidylserinesReceptors, Cytoplasmic and NuclearRecombinant Proteinslipid clusteringmolecular dynamicsPH domainsurface plasmon resonanceX-ray crystallography

Identifiers

PMID27974389
PMCPMC5290484
OpenAlexW2562759203

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.