TY - JOUR U1 - Zeitschriftenartikel, wissenschaftlich - begutachtet (reviewed) A1 - Bernardi, Austen A1 - Kirschner, Karl N. A1 - Faller, Roland T1 - Structural analysis of human glycoprotein butyrylcholinesterase using atomistic molecular dynamics: The importance of glycosylation site ASN241 JF - PLoS ONE N2 - 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. UN - https://nbn-resolving.org/urn:nbn:de:hbz:1044-opus-34334 SN - 1932-6203 SS - 1932-6203 U6 - https://doi.org/10.1371/journal.pone.0187994 DO - https://doi.org/10.1371/journal.pone.0187994 PM - 29190644 VL - 12 IS - 11 SP - 17 S1 - 17 PB - Public Library of Science (PLoS) CY - San Francisco, CA, USA ER -