Evidence map›Paper›PMID 30388104›Full record

ArticlePLoS computational biology2018

Demonstrating aspects of multiscale modeling by studying the permeation pathway of the human ZnT2 zinc transporter.

Yarden Golan, Raphael Alhadeff, Fabian Glaser, Assaf Ganoth, Arieh Warshel, Yehuda G Assaraf

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in PLoS computational biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

6 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 2 countries.

Yarden GolanThe Fred Wyszkowski Cancer Research Laboratory, Dept. of Biology, Technion-Israel Institute of Technology, Haifa, Israel.ORCID 0000-0002-3043-3638
Raphael AlhadeffDepartment of Chemistry, University of Southern California, Los Angeles, CA, United States of America.
Fabian GlaserLorry I. Lokey Interdisciplinary Center for Life Sciences and Engineering, Technion-Israel Institute of Technology, Haifa, Israel.
Assaf GanothThe Interdisciplinary Center (IDC), Herzliya, Israel.
Arieh WarshelDepartment of Chemistry, University of Southern California, Los Angeles, CA, United States of America.
Yehuda G AssarafThe Fred Wyszkowski Cancer Research Laboratory, Dept. of Biology, Technion-Israel Institute of Technology, Haifa, Israel.ORCID 0000-0001-6692-8221
Technion – Israel Institute of Technology · ILUniversity of Southern California · USReichman University · IL

Funding

Multiscale Simulations of Biological Systems and ProcessesR35GM122472 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI ARIEH WARSHEL · 2017 to 2026
$5.0M
SV40 T Antigen Structure and Helicase MechanismsR01AI055926 · NIAID · UNIVERSITY OF SOUTHERN CALIFORNIA · PI CHEN, XIAOJIANG S · 2004 to 2013
$4.0M
NIAID NIH HHS R01 AI055926NIGMS NIH HHS R35 GM122472
6 · The paper itself

Abstract

Multiscale modeling provides a very powerful means of studying complex biological systems. An important component of this strategy involves coarse-grained (CG) simplifications of regions of the system, which allow effective exploration of complex systems. Here we studied aspects of CG modeling of the human zinc transporter ZnT2. Zinc is an essential trace element with 10% of the proteins in the human proteome capable of zinc binding. Thus, zinc deficiency or impairment of zinc homeostasis disrupt key cellular functions. Mammalian zinc transport proceeds via two transporter families: ZnT and ZIP; however, little is known about the zinc permeation pathway through these transporters. As a step towards this end, we herein undertook comprehensive computational analyses employing multiscale techniques, focusing on the human zinc transporter ZnT2 and its bacterial homologue, YiiP. Energy calculations revealed a favorable pathway for zinc translocation via alternating access. We then identified key residues presumably involved in the passage of zinc ions through ZnT2 and YiiP, and functionally validated their role in zinc transport using site-directed mutagenesis of ZnT2 residues. Finally, we use a CG Monte Carlo simulation approach to sample the transition between the inward-facing and the outward-facing states. We present our structural models of the inward- and outward-facing conformations of ZnT2 as a blueprint prototype of the transporter conformations, including the putative permeation pathway and participating residues. The insights gained from this study may facilitate the delineation of the pathways of other zinc transporters, laying the foundations for the molecular basis underlying ion permeation. This may possibly facilitate the development of therapeutic interventions in pathological states associated with zinc deficiency and other disorders based on loss-of-function mutations in solute carriers.

Indexed as

Models, TheoreticalCation Transport ProteinsComputational BiologyDeficiency DiseasesHomeostasisHumansMonte Carlo MethodMutagenesis, Site-DirectedPermeabilityZincCation Transport ProteinsSLC30A2 protein, humanZinc

Identifiers

PMID30388104
PMCPMC6241132
OpenAlexW2898808132

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.