Please use this identifier to cite or link to this item:
https://hdl.handle.net/20.500.12202/3996
Title: | The Role of Glycosylation in the Autocleavage of Human γGlutamyl Transpeptidase 1 |
Authors: | Shulman, Avital |
Keywords: | Glycosylation Transglutaminases Glycoproteins -- Synthesis |
Issue Date: | 18-Apr-2016 |
Publisher: | Stern College for Women |
Abstract: | N-glycosylation is a widely occurring post-translational modification in which an oligosaccharide is linked to the amide nitrogen of an Asn side chain in the sequence Asn-XThr/Ser (where X≠Pro). This modification has been shown to play a role in protein folding, trafficking, stability, and function. Here we use molecular dynamics simulations of glycosylated and unglycosylated structures to address the role of N-glycosylation in the regulation of enzymatic function in human γ-Glutamyltranspeptidase 1 (hGGT1; EC 2.3.2.2). hGGT1 is a conserved enzyme known to play a role in maintaining cysteine levels in the body and in regulating intra-cellular redox status. The crystal structure of hGGT1 indicates that it is post-translationally modified by N-glycosylation at seven sites, and glycosylation at N95 has been shown to be the most critical to the ability of the enzyme to undergo activation through autocatalysis. |
Description: | The file is restricted for YU community access only. |
URI: | https://hdl.handle.net/20.500.12202/3996 https://ezproxy.yu.edu/login?url=https://repository.yu.edu/handle/20.500.12202/3996 |
Appears in Collections: | S. Daniel Abraham Honors Student Theses |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
Avital-Shulman.pdf Restricted Access | 690.23 kB | Adobe PDF | View/Open |
This item is licensed under a Creative Commons License