Disulfide bond as a structural determinant of prion protein membrane insertion
- Authors
- Shin, JY[Shin, Jae Yoon]; Shin, JI[Shin, Jae Il]; Kim, JS[Kim, Jun Seob]; Yang, YS[Yang, Yoo Soo]; Shin, YK[Shin, Yeon-Kyun]; Kim, KK[Kim, Kyeong Kyu]; Lee, S[Lee, Sangho]; Kweon, DH[Kweon, Dae-Hyuk]
- Issue Date
- Jun-2009
- Publisher
- KOREAN SOC MOLECULAR & CELLULAR BIOLOGY
- Keywords
- disulfide bond; membrane binding; prion protein; transmembrane domain
- Citation
- MOLECULES AND CELLS, v.27, no.6, pp.673 - 680
- Indexed
- SCIE
SCOPUS
KCI
- Journal Title
- MOLECULES AND CELLS
- Volume
- 27
- Number
- 6
- Start Page
- 673
- End Page
- 680
- URI
- https://scholarworks.bwise.kr/skku/handle/2021.sw.skku/77683
- DOI
- 10.1007/s10059-009-0089-9
- ISSN
- 1016-8478
- Abstract
- Conversion of the normal soluble form of prion protein, PrP (PrP(C)), to proteinase K-resistant form (PrP(Sc)) is a common molecular etiology of prion diseases. Proteinase K-resistance is attributed to a drastic conformational change from alpha-helix to beta-sheet and subsequent fibril formation. Compelling evidence suggests that membranes play a role in the conformational conversion of PrP. However, biophysical mechanisms underlying the conformational changes of PrP and membrane binding are still elusive. Recently, we demonstrated that the putative transmembrane domain (TMD; residues 111-135) of Syrian hamster PrP penetrates into the membrane upon the reduction of the conserved disulfide bond of PrP. To understand the mechanism underlying the membrane insertion of the TMD, here we explored changes in conformation and membrane binding abilities of PrP using wild type and cysteine-free mutant. We show that the reduction of the disulfide bond of PrP removes motional restriction of the TMD, which might, in turn, expose the TMD into solvent. The released TMD then penetrates into the membrane. We suggest that the disulfide bond regulates the membrane binding mode of PrP by controlling the motional freedom of the TMD.
- Files in This Item
- There are no files associated with this item.
- Appears in
Collections - Biotechnology and Bioengineering > Department of Genetic Engineering > 1. Journal Articles
- Medicine > Department of Medicine > 1. Journal Articles
- Science > Department of Biological Science > 1. Journal Articles
- Biotechnology and Bioengineering > Integrative Biotechnology > 1. Journal Articles
![qrcode](https://api.qrserver.com/v1/create-qr-code/?size=55x55&data=https://scholarworks.bwise.kr/skku/handle/2021.sw.skku/77683)
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.