Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/69099
Title: Structural and functional studies of leukemia-associated mutations in human cytosolic 5'-nucleotidase II
Authors: Lim, Pei Yiing
Keywords: DRNTU::Science
Issue Date: 2016
Abstract: NT5C2 relapse-associated mutations, K359Q and R367Q, are correlated with large gains in their enzymatic profiles. Crystal structures obtained in this study provide insights to the allosteric regulation mechanism of the enzyme by the disorder-to-order transition of a regulatory helix, which forms part of the active site. In addition, the mutant enzymes possess an increased basal level of activity and sensitivity to activation by effectors. In this study, the structural aspects of how each mutation potentially gains an advantage over the wild-type protein is revealed, with supporting evidence from biochemical and biophysical assays.
URI: http://hdl.handle.net/10356/69099
Fulltext Permission: restricted
Fulltext Availability: With Fulltext
Appears in Collections:SBS Theses

Files in This Item:
File Description SizeFormat 
MSc_LimPeiYiing.pdf
  Restricted Access
21.83 MBAdobe PDFView/Open

Page view(s)

170
Updated on May 14, 2021

Download(s)

14
Updated on May 14, 2021

Google ScholarTM

Check

Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.