Copper binding sites in the C‐terminal domain of mouse prion protein: A hybrid (QM/MM) molecular dynamics study

2008 ◽  
Vol 70 (3) ◽  
pp. 1084-1098 ◽  
Author(s):  
Maria Carola Colombo ◽  
Joost VandeVondele ◽  
Sabine Van Doorslaer ◽  
Alessandro Laio ◽  
Leonardo Guidoni ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Prion Protein ◽  
Binding Sites ◽  
Protein A ◽  
Copper Binding ◽  
Terminal Domain ◽  
Copper Binding Sites

scholarly journals Interactions between Copper-binding Sites Determine the Redox Status and Conformation of the Regulatory N-terminal Domain of ATP7B

2009 ◽  
Vol 285 (9) ◽  
pp. 6327-6336 ◽  
Author(s):  
Erik S. LeShane ◽  
Ujwal Shinde ◽  
Joel M. Walker ◽  
Amanda N. Barry ◽  
Ninian J. Blackburn ◽  
...  
Keyword(s):  
Binding Sites ◽  
Redox Status ◽  
Copper Binding ◽  
Terminal Domain ◽  
Copper Binding Sites

scholarly journals Molecular Features of the Copper Binding Sites in the Octarepeat Domain of the Prion Protein†

Biochemistry ◽  
2002 ◽  
Vol 41 (12) ◽  
pp. 3991-4001 ◽  
Author(s):  
Colin S. Burns ◽  
Eliah Aronoff-Spencer ◽  
Christine M. Dunham ◽  
Paula Lario ◽  
Nikolai I. Avdievich ◽  
...  
Keyword(s):  
Prion Protein ◽  
Binding Sites ◽  
Copper Binding ◽  
Molecular Features ◽  
Copper Binding Sites

Combination of Copper Ions and Nucleotide Generates Aggregates from Prion Protein Fragments in the N-Terminal Domain

2020 ◽  
Vol 27 (8) ◽  
pp. 782-792
Author(s):  
Noriyuki Shiraishi ◽  
Yoshiaki Hirano
Keyword(s):  
Binding Sites ◽  
Copper Ions ◽  
Adenine Nucleotides ◽  
Proteinase K ◽  
Copper Binding ◽  
Pyridine Nucleotides ◽  
Protein Fragments ◽  
Terminal Domain ◽  
Ribose Moiety ◽  
Copper Binding Sites

Background: It has been previously found that PrP23-98, which contains four highly conserved octarepeats (residues 60-91) and one partial repeat (residues 92-96), polymerizes into amyloid-like and proteinase K-resistant spherical aggregates in the presence of NADPH plus copper ions. Objective: We aimed to determine the requirements for the formation of these aggregates. Methods: In this study, we performed an aggregation experiment using N-acetylated and Camidated PrP fragments of the N-terminal domain, Octa1, Octa2, Octa3, Octa4, PrP84−114, and PrP76−114, in the presence of NADPH with copper ions, and focused on the effect of the number of copper-binding sites on aggregation. Results: Among these PrP fragments, Octa4, containing four copper-binding sites, was particularly effective in forming aggregates. We also tested the effect of other pyridine nucleotides and adenine nucleotides on the aggregation of Octa4. ATP was equally effective, but NADH, NADP, ADP, and AMP had no effect. Conclusion: The phosphate group on the adenine-linked ribose moiety of adenine nucleotides and pyridine nucleotides is presumed to be essential for the observed effect on aggregation. Efficient aggregation requires the presence of the four octarepeats. These insights may be helpful in the eventual development of therapeutic agents against prion-related disorders.

scholarly journals Mutation of copper binding sites on cellular prion protein abolishes its inhibitory action on NMDA receptors in mouse hippocampal neurons

2021 ◽  
Vol 14 (1) ◽  
Author(s):  
Sun Huang ◽  
Stefanie A. Black ◽  
Junting Huang ◽  
Peter K. Stys ◽  
Gerald W. Zamponi
Keyword(s):  
Nmda Receptor ◽  
Prion Protein ◽  
Binding Sites ◽  
Hippocampal Neurons ◽  
Primary Cultures ◽  
Cellular Prion Protein ◽  
Null Mouse ◽  
Dependent Manner ◽  
Copper Binding ◽  
Copper Binding Sites

AbstractWe have previously reported that cellular prion protein (PrPC) can down-regulate NMDA receptor activity and in a copper dependent manner. Here, we employed AAV9 to introduce murine cellular prion protein into mouse hippocampal neurons in primary cultures from PrP null mice to determine the role of the six copper binding motifs located within the N-terminal domain of PrPC. The results demonstrate that viral expression of wild type PrPC lowers NMDAR activity in PrP null mouse hippocampal neurons by reducing the magnitude of non-desensitizing currents. Elimination of the last two copper binding sites alone, or in combination with the remaining four attenuates this protective effect. Thus our data suggest that copper ion interactions with specific binding sites on PrPC are critical for PrPC dependent modulation of NMDA receptor function.

Unraveling the Cu2+Binding Sites in the C-Terminal Domain of the Murine Prion Protein:  A Pulse EPR and ENDOR Study†

2001 ◽  
Vol 105 (8) ◽  
pp. 1631-1639 ◽  
Author(s):  
Sabine Van Doorslaer ◽  
Grazia M. Cereghetti ◽  
Rudi Glockshuber ◽  
Arthur Schweiger
Keyword(s):  
Prion Protein ◽  
Binding Sites ◽  
Protein A ◽  
Terminal Domain ◽  
Pulse Epr

Determination of copper binding sites in peptides containing basic residues: a combined experimental and theoretical study

2001 ◽  
Vol 204 (1-3) ◽  
pp. 31-46 ◽  
Author(s):  
Brian K. Bluhm ◽  
Sharon J. Shields ◽  
Craig A. Bayse ◽  
Michael B. Hall ◽  
David H. Russell
Keyword(s):  
Binding Sites ◽  
Theoretical Study ◽  
Copper Binding ◽  
Determination Of Copper ◽  
Copper Binding Sites

Scaffolded amino acids as a close structural mimic of type-3 copper binding sites

2007 ◽  
pp. 4895 ◽  
Author(s):  
H. Bauke Albada ◽  
Fouad Soulimani ◽  
Bert M. Weckhuysen ◽  
Rob M. J. Liskamp
Keyword(s):  
Amino Acids ◽  
Binding Sites ◽  
Copper Binding ◽  
Type 3 ◽  
Copper Binding Sites

scholarly journals Measurement of Copper-Binding Sites on Low Density Lipoprotein

2001 ◽  
Vol 21 (4) ◽  
pp. 594-602 ◽  
Author(s):  
Alexander Roland ◽  
Rebecca A. Patterson ◽  
David S. Leake
Keyword(s):  
Binding Sites ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Low Density ◽  
Copper Binding ◽  
Copper Binding Sites
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