Open AccessStructural analysis of human glycoprotein butyrylcholinesterase using atomistic molecular dynamics: The importance of glycosylation site ASN241
Author(s) -
Austen Bernardi,
Karl N. Kirschner,
Roland Faller
Publication year - 2017
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0187994
Subject(s) - butyrylcholinesterase , glycosylation , glycan , glycoprotein , chemistry , biochemistry , n linked glycosylation , enzyme , acetylcholinesterase , aché
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 ASN 241 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 ASN 241 , monomeric human BChE glycoforms were simulated with and without site ASN 241 glycosylated. Our simulations indicate that the structure and function of human BChE are significantly affected by the absence of glycan 241.