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Identification of a potential allosteric site of Golgi α-mannosidase II using computer-aided drug design
- Source :
- PLoS ONE, PLoS ONE, Vol 14, Iss 5, p e0216132 (2019)
- Publication Year :
- 2019
- Publisher :
- PLOS, 2019.
-
Abstract
- Golgi α-mannosidase II (GMII) is a glycoside hydrolase playing a crucial role in the N-glycosylation pathway. In various tumour cell lines, the distribution of N-linked sugars on the cell surface is modified and correlates with the progression of tumour metastasis. GMII therefore is a possible molecular target for anticancer agents. Here, we describe the identification of a non-competitive GMII inhibitor using computer-aided drug design methods including identification of a possible allosteric binding site, pharmacophore search and virtual screening. publishedVersion
- Subjects :
- Hydrolases
Golgi Apparatus
Physical Chemistry
Biochemistry
570 Life sciences
Isomers
Binding Analysis
Stereochemistry
Stereoisomers
Cloning, Molecular
Drosophila Melanogaster
Eukaryota
Animal Models
Recombinant Proteins
Enzymes
Insects
Molecular Docking Simulation
Chemistry
Bioassays and Physiological Analysis
Experimental Organism Systems
Physical Sciences
Medicine
Drosophila
Allosteric Site
Research Article
570 Biowissenschaften
Arthropoda
Glycoside Hydrolases
Science
Research and Analysis Methods
Model Organisms
Isomerism
alpha-Mannosidase
Animals
Protein Structure, Quaternary
Chemical Characterization
Enzyme Assays
Binding Sites
Chemical Bonding
Organisms
Chemical Compounds
Biology and Life Sciences
Proteins
Hydrogen Bonding
Invertebrates
Drug Design
Enzyme Structure
Animal Studies
Enzymology
Electrostatic Bonding
Biochemical Analysis
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Journal :
- PLoS ONE, PLoS ONE, Vol 14, Iss 5, p e0216132 (2019)
- Accession number :
- edsair.doi.dedup.....d5f845f3d448a03aa52245b5e3b8079d
- Full Text :
- https://doi.org/10.25358/openscience-154