Evidence map›Paper›PMID 17357155›Full record

ArticleProteins2007

Homology modeling and molecular dynamics simulations of the glycine receptor ligand binding domain.

Kirill Speranskiy, Michael Cascio, Maria Kurnikova

Open access · greenAbstract read
In one paragraph

Article in Proteins, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed, 25 citations in OpenAlex.

  1. The neural γJournal of molecular modeling · 2018
    Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
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  10. Article
  11. Structural answers and persistent questions about how nicotinic receptors work.Frontiers in bioscience : a journal and virtual library · 2008
    Review
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.

Kirill SperanskiyDepartment of Chemistry, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213, USA.
Michael Cascio
Maria Kurnikova
Carnegie Mellon University · USUniversity of Pittsburgh · US

Funding

Hierarchical Modeling/Ion Channel and Receptor MechanismR01GM067962 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI KURNIKOVA, MARIA G · 2005 to 2009
$1.0M
NIGMS NIH HHS R01 GM067962
6 · The paper itself

Abstract

We present a homology based model of the ligand binding domain (LBD) of the homopentameric alpha1 glycine receptor (GlyR). The model is based on multiple sequence alignment with other members of the nicotinicoid ligand gated ion channel superfamily and two homologous acetylcholine binding proteins (AChBP) from the freshwater (Lymnaea stagnalis) and saltwater (Aplysia californica) snails with known high resolution structure. Using two template proteins with known structure to model three dimensional structure of a target protein is especially advantageous for sequences with low homology as in the case presented in this paper. The final model was cross-validated by critical evaluation of experimental and published mutagenesis, functional and other biochemical studies. In addition, a complex structure with strychnine antagonist in the putative binding site is proposed based on docking simulation using Autodock program. Molecular dynamics (MD) simulations with simulated annealing protocol are reported on the proposed LBD of GlyR, which is stable in 5 ns simulation in water, as well as for a deformed LBD structure modeled on the corresponding domain determined in low-resolution cryomicroscopy structure of the alpha subunit of the full-length acetylcholine receptor (AChR). Our simulations demonstrate that the beta-sandwich central core of the protein monomer is fairly rigid in the simulations and resistant to deformations in water.

Indexed as

Amino Acid SequenceBinding SitesComputer SimulationConserved SequenceLigandsModels, MolecularMolecular Sequence DataProtein BindingProtein Structure, QuaternaryProtein Structure, TertiaryProtein SubunitsReceptors, GlycineSequence AlignmentStructural Homology, ProteinLigandsProtein SubunitsReceptors, Glycine

Identifiers

PMID17357155
PMCPMC2873197
OpenAlexW2008698030

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.