Detailed computational analysis revealed mutation V210I on PrP induced conformational conversion on β2–α2 loop and α2

Detailed computational analysis revealed mutation V210I on PrP induced conformational conversion on β2–α2 loop and α2–α3

Published:2016 Issue:10 Volume:12 Page:3223-3233
ISSN:1742-206X
Container-title:Molecular BioSystems
language:en
Short-container-title:Mol. BioSyst.

Author:

Chandrasekaran P.¹²³⁴⁵,Rajasekaran R.¹²³⁴⁵

Affiliation:

1. Computational Biology Lab

2. Department of Biotechnology

3. School of Biosciences and Technology

4. VIT University

5. Vellore 632 014

Abstract

The development of fatal transmissible spongiform encephalopathies (TSE) is associated with the conformational conversion of the normal cellular prion protein, PrP^C, into its pathogenic isoform, PrP^Sc.

Publisher

Royal Society of Chemistry (RSC)

Subject

Molecular Biology,Biotechnology

Link

http://pubs.rsc.org/en/content/articlepdf/2016/MB/C6MB00342G

Reference54 articles.

1. Detailed computational analysis revealed mutation V210I on PrP induced conformational conversion on β2–α2 loop and α2–α3

2. 2-Microglobulin isoforms display an heterogeneous affinity for type I collagen

3. Detailed Biophysical Characterization of the Acid-Induced PrPc to PrPβ Conversion Process

4. Diverse Effects on the Native β-Sheet of the Human Prion Protein Due to Disease-Associated Mutations

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