The complex-formation behaviour of His residues in the fifth Cu2+ binding site of human prion protein: a close look

2009 ◽  
Vol 33 (11) ◽  
pp. 2300 ◽  
Author(s):  
Maurizio Remelli ◽  
Daniela Valensin ◽  
Dimitri Bacco ◽  
Ewa Gralka ◽  
Remo Guerrini ◽  
...  
Keyword(s):  
Complex Formation ◽  
Binding Site ◽  
Prion Protein ◽  
Protein A ◽  
Human Prion Protein

Prevalent Mutations of Human Prion Protein: A Molecular Modeling and Molecular Dynamics Study

2011 ◽  
Vol 29 (2) ◽  
pp. 379-389 ◽  
Author(s):  
Esmaeil Behmard ◽  
Parviz Abdolmaleki ◽  
Ebrahim Barzegari Asadabadi ◽  
Samad Jahandideh
Keyword(s):  
Molecular Dynamics ◽  
Molecular Modeling ◽  
Prion Protein ◽  
Protein A ◽  
Human Prion Protein

Effects of the Pathological Q212P Mutation on Human Prion Protein Non-Octarepeat Copper-Binding Site

Biochemistry ◽  
2012 ◽  
Vol 51 (31) ◽  
pp. 6068-6079 ◽  
Author(s):  
Paola D’Angelo ◽  
Stefano Della Longa ◽  
Alessandro Arcovito ◽  
Giordano Mancini ◽  
Andrea Zitolo ◽  
...  
Keyword(s):  
Binding Site ◽  
Prion Protein ◽  
Copper Binding ◽  
Human Prion Protein

scholarly journals Effects of the Pathological E200K Mutation on Human Prion Protein: A Computational screening and Molecular Dynamic approach

2022 ◽  
Author(s):  
Fatemeh Rahimi Gharemirshamloo ◽  
Ranabir Majumder ◽  
Kourosh Bamdad ◽  
Fateme Frootan ◽  
Cemal Un
Keyword(s):  
Protein Structure ◽  
Prion Protein ◽  
Prion Disease ◽  
Protein A ◽  
Protein Structures ◽  
Resistance Mutations ◽  
Pathogenic Potential ◽  
Computational Screening ◽  
E200k Mutation ◽  
Human Prion Protein

Abstract The Human Prion protein gene (PRNP) is mapped to short arm of chromosome 20 (20pter-12). Prion disease is associated with mutations in the Prion Protein encoding gene sequence. The mutations that occur in the prion protein could be divided into two types based on their influence on pathogenic potential: 1. Mutations that cause disease. 2. Disease-resistance mutations. Earlier studies found that the mutation G127V in the PRNP increases protein stability, whereas the mutation E200K, which has the highest mutation rate in the Prion protein, causes Creutzfeldt–Jakob disease (CJD) in humans and induces protein aggregation. We used a variety of bioinformatic algorithms, including SIFT, PolyPhen, I-Mutant, PhD-SNP, and SNP&GO, to predict the association of the E200K mutation with Prion disease. MD simulation is performed and graphs for RMSD, RMSF, Rg, DSSP, PCA, porcupine and FEL are generated to confirm and prove the stability of the wild type and mutant protein structures. The protein is analyzed for aggregation, and the results indicates more fluctuations in the protein structure during the simulation by the E200K mutation, however the G127V mutation makes protein structure stable against aggregation during the simulation.

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