Evidence map›Paper›PMID 26837804›Full record

ArticleBiochemistry2016

Molecular Modeling of the Structural and Dynamical Changes in Calcium Channel TRPV5 Induced by the African-Specific A563T Variation.

Lingyun Wang, Ross P Holmes, Ji-Bin Peng

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

10 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
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  8. Activation mechanisms of αVβ3 integrin by binding to fibronectin: A computational study.Protein science : a publication of the Protein Society · 2017
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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

3 authors at 2 institutions in 1 country.

Lingyun WangDivision of Nephrology, Department of Medicine, Nephrology Research and Training Center and ‡Department of Urology, University of Alabama at Birmingham , Birmingham, Alabama 35294, United States.
Ross P HolmesDivision of Nephrology, Department of Medicine, Nephrology Research and Training Center and ‡Department of Urology, University of Alabama at Birmingham , Birmingham, Alabama 35294, United States.
Ji-Bin PengDivision of Nephrology, Department of Medicine, Nephrology Research and Training Center and ‡Department of Urology, University of Alabama at Birmingham , Birmingham, Alabama 35294, United States.
Pediatric Nephrology of Alabama · USUniversity of Alabama at Birmingham · US

Funding

Regulation of WNK4, a protein kinase mutated in a hereditary form of hypertensionR01DK072154 · NIDDK · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI PENG, JI-BIN · 2007 to 2017
$2.2M
NIDDK NIH HHS R01 DK072154NIDDK NIH HHS R01DK072154
6 · The paper itself

Abstract

Transient receptor potential cation channels, vanilloid subfamily, member 5 (TRPV5) plays a key role in active Ca(2+) reabsorption in the kidney. Variations in TRPV5 occur at high frequency in African populations and may contribute to their higher efficiency of Ca(2+) reabsorption. One of the African specific variations, A563T, exhibits increased Ca(2+) transport ability. However, it is unclear how this variation influences the channel pore. On the basis of the structure of TRPV1, a TRPV5 model was generated to simulate the structural and dynamical changes induced by the A563T variation. On the basis of this model, amino acid residue 563 interacts with V540, which is one residue away from the key residue, D542, involved in Ca(2+) selectivity and Mg(2+) blockade. The A563T variation increases secondary structure stability and reduces dynamical motion of D542. In addition, the A563T variation alters the electrostatic potential of the outer surface of the pore. Differences in contact between selective filter residues and residue 563 and in electrostatic potential between the two TRPV5 variants were also observed in another model derived from an alternative alignment in the selective filters between TRPV5 and TRPV1. These findings indicate that the A563T variation induces structural, dynamical, and electrostatic changes in the TRPV5 pore, providing structural insight into the functional alterations associated with the A563T variation.

Indexed as

Molecular Dynamics SimulationPoint MutationAnimalsBlack PeopleCalciumHumansProtein ConformationRatsStatic ElectricityTRPV Cation ChannelsCalciumTRPV5 protein, humanTRPV Cation Channels

Identifiers

PMID26837804
PMCPMC5304435
OpenAlexW2266688981

What OpenQuestion holds

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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.