Evidence map›Paper›PMID 21669869›Full record

ArticleThe Journal of biological chemistry2011

An undecided coiled coil: the leucine zipper of Nek2 kinase exhibits atypical conformational exchange dynamics.

Rebecca Croasdale, Frank J Ivins, Fred Muskett, Tina Daviter, David J Scott, Tara Hardy, Steven J Smerdon, Andrew M Fry, Mark Pfuhl

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

26 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
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  6. Self-assembly of the bZIP transcription factor ΔFosB.Current research in structural biology · 2020
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  11. Review
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  16. Mitotic Regulation by NEK Kinase Networks.Frontiers in cell and developmental biology · 2017
    Review
  17. Coiled-coil destabilizing residues in the group A Streptococcus M1 protein are required for functional interaction.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  18. 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

9 authors at 4 institutions in 1 country.

Rebecca CroasdaleDepartment of Biochemistry, University of Leicester, Leicester LE1 9HN, United Kingdom.
Frank J Ivins
Fred Muskett
Tina Daviter
David J Scott
Tara Hardy
Steven J Smerdon
Andrew M Fry
Mark Pfuhl
University of Leicester · GBMedical Research Council · GBBirkbeck, University of London · GBUniversity of Nottingham · GB

Funding

Cancer Research UKMedical Research Council MC_U117584228Wellcome Trust
6 · The paper itself

Abstract

Leucine zippers are oligomerization domains used in a wide range of proteins. Their structure is based on a highly conserved heptad repeat sequence in which two key positions are occupied by leucines. The leucine zipper of the cell cycle-regulated Nek2 kinase is important for its dimerization and activation. However, the sequence of this leucine zipper is most unusual in that leucines occupy only one of the two hydrophobic positions. The other position, depending on the register of the heptad repeat, is occupied by either acidic or basic residues. Using NMR spectroscopy, we show that this leucine zipper exists in two conformations of almost equal population that exchange with a rate of 17 s(-1). We propose that the two conformations correspond to the two possible registers of the heptad repeat. This hypothesis is supported by a cysteine mutant that locks the protein in one of the two conformations. NMR spectra of this mutant showed the predicted 2-fold reduction of peaks in the (15)N HSQC spectrum and the complete removal of cross peaks in exchange spectra. It is possible that interconversion of these two conformations may be triggered by external signals in a manner similar to that proposed recently for the microtubule binding domain of dynein and the HAMP domain. As a result, the leucine zipper of Nek2 kinase is the first example where the frameshift of coiled-coil heptad repeats has been directly observed experimentally.

Indexed as

Leucine ZippersBase SequenceCircular DichroismDNA PrimersHumansMutagenesis, Site-DirectedNIMA-Related KinasesNuclear Magnetic Resonance, BiomolecularProtein ConformationProtein Serine-Threonine KinasesUltracentrifugationDNA PrimersNEK2 protein, humanNIMA-Related KinasesProtein Serine-Threonine Kinases

Identifiers

PMID21669869
PMCPMC3149346
OpenAlexW2022751822

What OpenQuestion holds

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LicenceCC BY-NC
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.