Detecting early stage structural changes in wild type, pathogenic and non-pathogenic prion variants using Markov state model.

ABSTRACT: The conversion of prion protein from normal to scrapie followed by the aggregation and deposition of this scrapie form leads to various neurodegenerative diseases. A few studies carried out by researchers suggest that E219K prion mutant (glutamate to lysine mutation at residue position 219) is more stable than wild type protein. However a similar point mutation E200K (glutamate to lysine mutation at residue position 200) is pathogenic. In this study we have carried out detailed atomistic simulation of the wild type, pathogenic mutant E200K and E219K mutant which provides more stability. The aim of the study was to detect the early structural changes present in all the three variants which might be responsible for the stability or for their conversion from PrPC to PrPSc. MSM based analyses

SUBMITTER: Jani V 

PROVIDER: S-EPMC9064127 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature