Evidence map›Paper›PMID 17095602›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

Surface comparison of active and inactive protein kinases identifies a conserved activation mechanism.

Alexandr P Kornev, Nina M Haste, Susan S Taylor, Lynn F Ten Eyck

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 384 papers.

0numbers the graph read from it
0cells of the map it votes in
384citing papers in PubMed
11.4field-weighted citation impact, top 1% 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

384 citing papers in PubMed, 754 citations in OpenAlex.

  1. Article
  2. A Constellation of Fluorescent Biosensors to Illuminate the Galaxy of Protein Kinases.Chembiochem : a European journal of chemical biology · 2026
    Review
  3. Article
  4. A PKA-selective inhibitor captures an open but more ordered conformation of the PKA catalytic subunit.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
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  12. Article
  13. Review
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  18. Local and distal changes in dynamics are caused by an L205R Cushing's syndrome mutant in PRKACA.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  19. Article
  20. Article

324 more citing papers are in PubMed but not listed here.

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

4 authors at 2 institutions in 1 country.

Alexandr P KornevSan Diego Supercomputer Center, University of California at San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA.
Nina M Haste
Susan S Taylor
Lynn F Ten Eyck
San Diego Supercomputer Center · USHoward Hughes Medical Institute · US

Funding

Protein Kinase: Primary Structure and cAMP InteractionsR01GM019301 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TAYLOR, SUSAN S. · 1985 to 2013
$3.4M
PROTEIN KINASE: PRIMARY STRUCTURE AND CAMP INTERACTIONR37GM019301 · NIGMS · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI TAYLOR, SUSAN S · 1995 to 2004
$2.0M
Computation and Mass Spec: Predicting Protein ComplexesR01GM070996 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TEN EYCK, LYNN F. · 2004 to 2007
$1.3M
NIGMS NIH HHS GM19301NIGMS NIH HHS GM70996NIGMS NIH HHS R01 GM019301NIGMS NIH HHS R01 GM070996NIGMS NIH HHS R37 GM019301
6 · The paper itself

Abstract

The surface comparison of different serine-threonine and tyrosine kinases reveals a set of 30 residues whose spatial positions are highly conserved. The comparison between active and inactive conformations identified the residues whose positions are the most sensitive to activation. Based on these results, we propose a model of protein kinase activation. This model explains how the presence of a phosphate group in the activation loop determines the position of the catalytically important aspartate in the Asp-Phe-Gly motif. According to the model, the most important feature of the activation is a "spine" formation that is dynamically assembled in all active kinases. The spine is comprised of four hydrophobic residues that we detected in a set of 23 eukaryotic and prokaryotic kinases. It spans the molecule and plays a coordinating role in activated kinases. The spine is disordered in the inactive kinases and can explain how stabilization of the whole molecule is achieved upon phosphorylation.

Indexed as

AlgorithmsEnzyme ActivationAmino Acid SequenceCyclic AMP-Dependent Protein KinasesCyclin-Dependent Kinase 2HumansHydrophobic and Hydrophilic InteractionsModels, MolecularPhosphorylationProtein Structure, TertiaryCyclic AMP-Dependent Protein KinasesCyclin-Dependent Kinase 2

Identifiers

PMID17095602
PMCPMC1693824
OpenAlexW2000390423

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.