Molecular dynamics study of the Cu2+ binding-induced "structuring" of the N-terminal domain of human prion protein.
In this work, we report molecular dynamics simulations on a fragment of the human prion protein spanning residues 31-120, with copper(II) bound to the repeat region in several ways corresponding to the known intra- and inter-repeat coordination modes, or to the metal site located at His111. The results of this study point to a different structuring tendency of the protein fragment depending on copper binding mode, with the highest degree of structuring in the case of intrarepeat Cu(II) coordination corresponding to high copper concentration.
Valensin
Gianni
G
Molteni
Elena
E
Valensin
Daniela
D
Taraszkiewicz
Magdalena
M
Kozlowski
Henryk
H
D003198:Computer Simulation; D003300:Copper / Q000737:chemistry*; D006639:Histidine / Q000737:chemistry; D006801:Humans; D021962:Membrane Microdomains / Q000737:chemistry; D008958:Models, Molecular; D011328:Prions / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation
D011328:Prions; D006639:Histidine; D003300:Copper