Echinomycin, a potential binder of FKBP12, shows minor effect on calcineurin activity.
Identifieur interne : 000E02 ( Main/Corpus ); précédent : 000E01; suivant : 000E03Echinomycin, a potential binder of FKBP12, shows minor effect on calcineurin activity.
Auteurs : Vikramjeet Singh ; Amita Nand ; Caixia Chen ; Zhipeng Li ; Sheng-Jie Li ; Songbai Wang ; Mo Yang ; Alejandro Merino ; Lixin Zhang ; Jingsong ZhuSource :
- Journal of biomolecular screening [ 1552-454X ] ; 2014.
English descriptors
- KwdEn :
- Calcineurin (chemistry), Calcineurin (metabolism), Echinomycin (chemistry), Echinomycin (metabolism), Echinomycin (pharmacology), Enzyme Activation (drug effects), Models, Biological (MeSH), Models, Molecular (MeSH), Molecular Conformation (MeSH), Molecular Docking Simulation (MeSH), Phosphoric Monoester Hydrolases (metabolism), Protein Binding (MeSH), Reproducibility of Results (MeSH), Signal Transduction (drug effects), Surface Plasmon Resonance (methods), Tacrolimus Binding Protein 1A (metabolism).
- MESH :
- chemical , chemistry : Calcineurin, Echinomycin.
- chemical , metabolism : Calcineurin, Echinomycin, Phosphoric Monoester Hydrolases, Tacrolimus Binding Protein 1A.
- chemical , pharmacology : Echinomycin.
- drug effects : Enzyme Activation, Signal Transduction.
- methods : Surface Plasmon Resonance.
- Models, Biological, Models, Molecular, Molecular Conformation, Molecular Docking Simulation, Protein Binding, Reproducibility of Results.
Abstract
Echinomycin, a member of the quinoxaline family of antibiotics, is known to be a small-molecule inhibitor of hypoxia inducible factor-1 (HIF-1) DNA binding activity. Recently, it has been shown to suppress mammalian target of rapamycin (mTOR) signaling and growth in leukemia cell lines. In this study, we investigated whether echinomycin interacts with the FKBP12 protein. Molecular docking was used, and the predicted binding energy was -10.61 kcal/mol. Moreover, surface plasmon resonance imaging and fluorescence quenching techniques were used to validate this interaction. Echinomycin binds to FKBP12 with a strong binding affinity comparable with rapamycin. Furthermore, the echinomycin-FKBP12 complex has been shown to affect calcineurin activity when tested in a calcineurin phosphatase inhibition assay. All of these studies have shown that echinomycin may have a double impact on HIF signaling by direct inhibition and through mTOR.
DOI: 10.1177/1087057114544742
PubMed: 25085862
Links to Exploration step
pubmed:25085862Le document en format XML
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<term>Echinomycin (chemistry)</term>
<term>Echinomycin (metabolism)</term>
<term>Echinomycin (pharmacology)</term>
<term>Enzyme Activation (drug effects)</term>
<term>Models, Biological (MeSH)</term>
<term>Models, Molecular (MeSH)</term>
<term>Molecular Conformation (MeSH)</term>
<term>Molecular Docking Simulation (MeSH)</term>
<term>Phosphoric Monoester Hydrolases (metabolism)</term>
<term>Protein Binding (MeSH)</term>
<term>Reproducibility of Results (MeSH)</term>
<term>Signal Transduction (drug effects)</term>
<term>Surface Plasmon Resonance (methods)</term>
<term>Tacrolimus Binding Protein 1A (metabolism)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Calcineurin</term>
<term>Echinomycin</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Calcineurin</term>
<term>Echinomycin</term>
<term>Phosphoric Monoester Hydrolases</term>
<term>Tacrolimus Binding Protein 1A</term>
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<term>Signal Transduction</term>
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</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Models, Biological</term>
<term>Models, Molecular</term>
<term>Molecular Conformation</term>
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<front><div type="abstract" xml:lang="en">Echinomycin, a member of the quinoxaline family of antibiotics, is known to be a small-molecule inhibitor of hypoxia inducible factor-1 (HIF-1) DNA binding activity. Recently, it has been shown to suppress mammalian target of rapamycin (mTOR) signaling and growth in leukemia cell lines. In this study, we investigated whether echinomycin interacts with the FKBP12 protein. Molecular docking was used, and the predicted binding energy was -10.61 kcal/mol. Moreover, surface plasmon resonance imaging and fluorescence quenching techniques were used to validate this interaction. Echinomycin binds to FKBP12 with a strong binding affinity comparable with rapamycin. Furthermore, the echinomycin-FKBP12 complex has been shown to affect calcineurin activity when tested in a calcineurin phosphatase inhibition assay. All of these studies have shown that echinomycin may have a double impact on HIF signaling by direct inhibition and through mTOR. </div>
</front>
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<Abstract><AbstractText>Echinomycin, a member of the quinoxaline family of antibiotics, is known to be a small-molecule inhibitor of hypoxia inducible factor-1 (HIF-1) DNA binding activity. Recently, it has been shown to suppress mammalian target of rapamycin (mTOR) signaling and growth in leukemia cell lines. In this study, we investigated whether echinomycin interacts with the FKBP12 protein. Molecular docking was used, and the predicted binding energy was -10.61 kcal/mol. Moreover, surface plasmon resonance imaging and fluorescence quenching techniques were used to validate this interaction. Echinomycin binds to FKBP12 with a strong binding affinity comparable with rapamycin. Furthermore, the echinomycin-FKBP12 complex has been shown to affect calcineurin activity when tested in a calcineurin phosphatase inhibition assay. All of these studies have shown that echinomycin may have a double impact on HIF signaling by direct inhibition and through mTOR. </AbstractText>
<CopyrightInformation>© 2014 Society for Laboratory Automation and Screening.</CopyrightInformation>
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