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Insights from molecular dynamics simulation of human ceruloplasmin (ferroxidase enzyme) binding with biogenic monoamines
Human ceruloplasmin (hCP) is a multi-copper oxidase with ferroxidase and amine oxidase activities. Molecular dynamics simulation (MDS) and docking analysis of biogenic monoamines with ceruloplasmin explain the role of Asp1025, Glu935, Glu272, Glu232 and Glu230 together with the binding site water mo...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Biomedical Informatics
2019
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6900326/ https://www.ncbi.nlm.nih.gov/pubmed/31831958 http://dx.doi.org/10.6026/97320630015750 |
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author | Mukhopadhyay, Bishnu Prasad |
author_facet | Mukhopadhyay, Bishnu Prasad |
author_sort | Mukhopadhyay, Bishnu Prasad |
collection | PubMed |
description | Human ceruloplasmin (hCP) is a multi-copper oxidase with ferroxidase and amine oxidase activities. Molecular dynamics simulation (MDS) and docking analysis of biogenic monoamines with ceruloplasmin explain the role of Asp1025, Glu935, Glu272, Glu232 and Glu230 together with the binding site water molecules (referred as conserved water molecules) in the stabilization of neurotransmitter (Serotonin, Norepinephrine and Epinephrine) molecules within the binding cavity of hCP. Conserved water molecules are found at specific positions interacting with the protein structures that have sequence similarity. The ethylamine side chain nitrogen atom (N1) of neurotransmitter molecules interacts with water molecules in the binding cavity formed by Asp1025, Glu935 and Glu232 residues. These residues form an acidic triad mimicking a substrate binding cavity. The hydroxyl groups attached to the catechol ring of epinephrine and norepinephrine have been stabilized by Asp230 and Asp232 residues. Data suggests that the recognition of biogenic amines mediates through the N+(amine) ...Asp1025-His1026-Cu(Cis-His) path. The potential recognition path of biogenic monoamines to trinuclear copper cluster supported by active site water molecules (referred as conserved water molecules) is described in this report. |
format | Online Article Text |
id | pubmed-6900326 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Biomedical Informatics |
record_format | MEDLINE/PubMed |
spelling | pubmed-69003262019-12-12 Insights from molecular dynamics simulation of human ceruloplasmin (ferroxidase enzyme) binding with biogenic monoamines Mukhopadhyay, Bishnu Prasad Bioinformation Research Article Human ceruloplasmin (hCP) is a multi-copper oxidase with ferroxidase and amine oxidase activities. Molecular dynamics simulation (MDS) and docking analysis of biogenic monoamines with ceruloplasmin explain the role of Asp1025, Glu935, Glu272, Glu232 and Glu230 together with the binding site water molecules (referred as conserved water molecules) in the stabilization of neurotransmitter (Serotonin, Norepinephrine and Epinephrine) molecules within the binding cavity of hCP. Conserved water molecules are found at specific positions interacting with the protein structures that have sequence similarity. The ethylamine side chain nitrogen atom (N1) of neurotransmitter molecules interacts with water molecules in the binding cavity formed by Asp1025, Glu935 and Glu232 residues. These residues form an acidic triad mimicking a substrate binding cavity. The hydroxyl groups attached to the catechol ring of epinephrine and norepinephrine have been stabilized by Asp230 and Asp232 residues. Data suggests that the recognition of biogenic amines mediates through the N+(amine) ...Asp1025-His1026-Cu(Cis-His) path. The potential recognition path of biogenic monoamines to trinuclear copper cluster supported by active site water molecules (referred as conserved water molecules) is described in this report. Biomedical Informatics 2019-10-31 /pmc/articles/PMC6900326/ /pubmed/31831958 http://dx.doi.org/10.6026/97320630015750 Text en © 2019 Biomedical Informatics http://creativecommons.org/licenses/by/3.0/ This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License. |
spellingShingle | Research Article Mukhopadhyay, Bishnu Prasad Insights from molecular dynamics simulation of human ceruloplasmin (ferroxidase enzyme) binding with biogenic monoamines |
title | Insights from molecular dynamics simulation of human ceruloplasmin (ferroxidase enzyme) binding with biogenic monoamines |
title_full | Insights from molecular dynamics simulation of human ceruloplasmin (ferroxidase enzyme) binding with biogenic monoamines |
title_fullStr | Insights from molecular dynamics simulation of human ceruloplasmin (ferroxidase enzyme) binding with biogenic monoamines |
title_full_unstemmed | Insights from molecular dynamics simulation of human ceruloplasmin (ferroxidase enzyme) binding with biogenic monoamines |
title_short | Insights from molecular dynamics simulation of human ceruloplasmin (ferroxidase enzyme) binding with biogenic monoamines |
title_sort | insights from molecular dynamics simulation of human ceruloplasmin (ferroxidase enzyme) binding with biogenic monoamines |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6900326/ https://www.ncbi.nlm.nih.gov/pubmed/31831958 http://dx.doi.org/10.6026/97320630015750 |
work_keys_str_mv | AT mukhopadhyaybishnuprasad insightsfrommoleculardynamicssimulationofhumanceruloplasminferroxidaseenzymebindingwithbiogenicmonoamines |