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Study · In silico · 2006

2 results

Molecular dynamics simulation of human neurohypophyseal hormone receptors complexed with oxytocin-modeling of an activated state.

Slusarz MJ, Slusarz R, Ciarkowski J

Journal of peptide science : an official publication of the European Peptide Society1 Mar 2006Cited by 18 (Europe PMC)

PMID16114099 (opens in a new tab)DOI10.1002/psc.713 (opens in a new tab)PepBankPUB-16114099
Publisher pagePubMedAsk about this study
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Summary

The text of this summary is not shown here, because the article license does not allow reuse. Read it at the source (opens in a new tab)

Text rights: Publisher copyright. Results still quote short attributed sentences.

Results from this study2

2 results from studies that gave the peptide. No result from this study comes from people.

  1. 01Computer modelIn silicoMechanism

    In molecular dynamics models, oxytocin formed stabilizing interactions with conserved Gln residues in all receptor complexes.

    In plain wordsIn computer models, oxytocin was predicted to bind conserved glutamine residues in all three receptors.

    Peptide
    Oxytocin
    Outcome
    Not applicableStabilizing interactions with conserved Gln residues
    Study

    n: not reported in source

    Molecular dynamics models of OTR, V1aR and V2R complexes with oxytocin in a POPC bilayer
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    The stabilizing interactions with conserved Gln residues in all complexes were identified.
    1 context sentence
    Summary · context
    The 1 ns unconstrained molecular dynamics (MD) of three pairs of receptor-OT complexes (two complexes per each receptor) immersed in the fully hydrated 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidylcholine (POPC) lipid bilayer was conducted in the AMBER 7.0 force field.
  2. 02Computer modelIn silicoMechanism

    In molecular dynamics models, nonconserved hydrophobic residues were proposed as responsible for oxytocin receptor selectivity and ligand recognition.

    In plain wordsIn computer models, certain hydrophobic receptor residues were predicted to decide which receptor oxytocin prefers.

    Peptide
    Oxytocin
    Outcome
    Not applicableResidues proposed for OTR-OT selectivity
    Study

    n: not reported in source

    Molecular dynamics models of OTR, V1aR and V2R complexes with oxytocin in a POPC bilayer
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    The nonconserved hydrophobic residues were proposed as responsible for OTR-OT selectivity and ligand recognition.
    1 context sentence
    Summary · context
    The 1 ns unconstrained molecular dynamics (MD) of three pairs of receptor-OT complexes (two complexes per each receptor) immersed in the fully hydrated 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidylcholine (POPC) lipid bilayer was conducted in the AMBER 7.0 force field.

AI wrote and checked these results. AI can make mistakes, so check important results against the source.

Version history

PepBank keeps every version of the data on this study. Status changes from Retraction Watch, Europe PMC and Crossref are listed with their source.

  1. Version 2Current

    11 Oct 2026, 20:03 UTC

    Study results updated

  2. Version 1

    9 Oct 2026, 02:51 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

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