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Structural analysis of human glycoprotein butyrylcholinesterase using atomistic molecular dynamics: The importance of glycosylation site ASN241

  • Human butyrylcholinesterase (BChE) is a glycoprotein capable of bioscavenging toxic compounds such as organophosphorus (OP) nerve agents. For commercial production of BChE, it is practical to synthesize BChE in non-human expression systems, such as plants or animals. However, the glycosylation profile in these systems is significantly different from the human glycosylation profile, which could result in changes in BChE's structure and function. From our investigation, we found that the glycan attached to ASN241 is both structurally and functionally important due to its close proximity to the BChE tetramerization domain and the active site gorge. To investigate the effects of populating glycosylation site ASN241, monomeric human BChE glycoforms were simulated with and without site ASN241 glycosylated. Our simulations indicate that the structure and function of human BChE are significantly affected by the absence of glycan 241.

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Metadaten
Document Type:Article
Language:English
Author:Austen Bernardi, Karl N. Kirschner, Roland Faller
Parent Title (English):PLoS ONE
Volume:12
Issue:11
First Page:e0187994
ISSN:1932-6203
URN:urn:nbn:de:hbz:1044-opus-34334
DOI:https://doi.org/10.1371/journal.pone.0187994
Pubmed Id:http://www.ncbi.nlm.nih.gov/pubmed?term=29190644
Publisher:Public Library of Science (PLoS)
Place of publication:San Francisco, CA, USA
Publishing Institution:Hochschule Bonn-Rhein-Sieg
Date of first publication:2017/11/30
Note:
© 2017 Bernardi et al. This is an open access article distributed under the terms of the Creative Commons Attribution License.
Departments, institutes and facilities:Fachbereich Informatik
Dewey Decimal Classification (DDC):5 Naturwissenschaften und Mathematik / 54 Chemie / 540 Chemie und zugeordnete Wissenschaften
Entry in this database:2017/12/05
Licence (German):License LogoCreative Commons - CC BY - Namensnennung 4.0 International