Computational studies on prion proteins: effect of Ala(117)-->Val mutation. Export

@article{citeulike:3631613, abstract = {Molecular dynamics calculations demonstrated the conformational change in the prion protein due to Ala(117)-->Val mutation, which is related to Gerstmann-Str\"{a}ussler-Sheinker disease, one of the familial prion diseases. Three kinds of model structures of human and mouse prion proteins were examined: (model 1) nuclear magnetic resonance structures of human prion protein HuPrP (125-228) and mouse prion protein MoPrP (124-224), each having a globular domain consisting of three alpha-helices and an antiparallel beta-sheet; (model 2) extra peptides including Ala(117) (109-124 in HuPrP and 109-123 in MoPrP) plus the nuclear magnetic resonance structures of model 1; and (model 3) extra peptides including Val(117) (109-124 in HuPrP and 109-123 in MoPrP) plus the nuclear magnetic resonance structures of model 1. The results of molecular dynamics calculations indicated that the globular domains of models 1 and 2 were stable and that the extra peptide in model 2 tended to form a new alpha-helix. On the other hand, the globular domain of model 3 was unstable, and the beta-sheet region increased especially in HuPrP.}, author = {Okimoto, N. and Yamanaka, K. and Suenaga, A. and Hata, M. and Hoshino, T.}, citeulike-article-id = {3631613}, citeulike-linkout-0 = {http://www.biophysj.org/cgi/content/abstract/82/5/2746}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/11964260}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=11964260}, issn = {0006-3495}, journal = {Biophysical journal}, keywords = {computational, prion, structure}, month = {May}, number = {5}, pages = {2746--2757}, posted-at = {2008-11-21 03:25:54}, priority = {2}, title = {Computational studies on prion proteins: effect of Ala(117)-->Val mutation.}, url = {http://www.biophysj.org/cgi/content/abstract/82/5/2746}, volume = {82}, year = {2002} }

TY - JOUR ID - citeulike:3631613 L3 - citeulike-article-id:3631613 N2 - Molecular dynamics calculations demonstrated the conformational change in the prion protein due to Ala(117)-->Val mutation, which is related to Gerstmann-Sträussler-Sheinker disease, one of the familial prion diseases. Three kinds of model structures of human and mouse prion proteins were examined: (model 1) nuclear magnetic resonance structures of human prion protein HuPrP (125-228) and mouse prion protein MoPrP (124-224), each having a globular domain consisting of three alpha-helices and an antiparallel beta-sheet; (model 2) extra peptides including Ala(117) (109-124 in HuPrP and 109-123 in MoPrP) plus the nuclear magnetic resonance structures of model 1; and (model 3) extra peptides including Val(117) (109-124 in HuPrP and 109-123 in MoPrP) plus the nuclear magnetic resonance structures of model 1. The results of molecular dynamics calculations indicated that the globular domains of models 1 and 2 were stable and that the extra peptide in model 2 tended to form a new alpha-helix. On the other hand, the globular domain of model 3 was unstable, and the beta-sheet region increased especially in HuPrP. IS - 5 JF - Biophysical journal SN - 0006-3495 EP - 2757 TI - Computational studies on prion proteins: effect of Ala(117)-->Val mutation. VL - 82 SP - 2746 KW - computational KW - prion KW - structure AU - Okimoto, N AU - Yamanaka, K AU - Suenaga, A AU - Hata, M AU - Hoshino, T PY - 2002/05// UR - http://www.biophysj.org/cgi/content/abstract/82/5/2746 ER -