Evidence map›Paper›PMID 20436473›Full record

ArticleNature structural & molecular biology2010

Structures of apicomplexan calcium-dependent protein kinases reveal mechanism of activation by calcium.

Amy K Wernimont, Jennifer D Artz, Patrick Finerty, Yu-Hui Lin, Mehrnaz Amani, Abdellah Allali-Hassani, Guillermo Senisterra, Masoud Vedadi, Wolfram Tempel, Farrell Mackenzie and 4 more

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 116 papers.

0numbers the graph read from it
0cells of the map it votes in
116citing papers in PubMed
12.7field-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

116 citing papers in PubMed, 236 citations in OpenAlex.

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56 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

14 authors at 3 institutions in 2 countries.

Amy K WernimontStructural Genomics Consortium, University of Toronto, Toronto, Ontario, Canada.
Jennifer D Artz
Patrick Finerty
Yu-Hui Lin
Mehrnaz Amani
Abdellah Allali-Hassani
Guillermo Senisterra
Masoud Vedadi
Wolfram Tempel
Farrell Mackenzie
Irene Chau
Sebastian Lourido
L David Sibley
Raymond Hui
University of Toronto · CAStructural Genomics Consortium · CAWashington University in St. Louis · US

Funding

PROTEIN SECRETION &INTRACELLULAR SURVIVAL BY TOXOPLASMAR01AI034036 · NIAID · WASHINGTON UNIVERSITY · PI SIBLEY, L. DAVID · 1993 to 2019
$7.9M
DESIGNING SELECTIVE INHIBITORS OF CALCIUM-DEPENDENT KINASES IN PARASITESR01AI094098 · NIAID · WASHINGTON UNIVERSITY · PI SIBLEY, L. DAVID · 2012 to 2015
$1.6M
CIHRNIAID NIH HHS AI034036NIAID NIH HHS R01 AI034036NIAID NIH HHS R01 AI094098Wellcome Trust
6 · The paper itself

Abstract

Calcium-dependent protein kinases (CDPKs) have pivotal roles in the calcium-signaling pathway in plants, ciliates and apicomplexan parasites and comprise a calmodulin-dependent kinase (CaMK)-like kinase domain regulated by a calcium-binding domain in the C terminus. To understand this intramolecular mechanism of activation, we solved the structures of the autoinhibited (apo) and activated (calcium-bound) conformations of CDPKs from the apicomplexan parasites Toxoplasma gondii and Cryptosporidium parvum. In the apo form, the C-terminal CDPK activation domain (CAD) resembles a calmodulin protein with an unexpected long helix in the N terminus that inhibits the kinase domain in the same manner as CaMKII. Calcium binding triggers the reorganization of the CAD into a highly intricate fold, leading to its relocation around the base of the kinase domain to a site remote from the substrate binding site. This large conformational change constitutes a distinct mechanism in calcium signal-transduction pathways.

Indexed as

CalciumCalcium-Calmodulin-Dependent Protein KinasesCryptosporidium parvumCrystallography, X-RayEnzyme ActivationModels, MolecularProtein BindingProtein ConformationProtein KinasesToxoplasmaCalciumCalcium-Calmodulin-Dependent Protein KinasesProtein Kinases

Identifiers

PMID20436473
PMCPMC3675764
OpenAlexW2022304951

What OpenQuestion holds

Textmetadata
LicenceTDM
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.