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Contribution of a putative salt bridge and backbone dynamics in the structural instability of human prion protein upon R208H mutation.

Abstract：

:Molecular dynamics simulation method is used to assess the contribution of a disease-associated salt bridge in the early stages of the conformational rearrangement of human prion protein upon Arg208-->His mutation, which causes Creutzfeldt-Jakob disease. Previous investigations have suggested that the breakage of this putative salt bridge (D144/E146<-->Arg208) between helix 1 and helix 3 is responsible for such a mutation-driven process. So far, no experimental data has been reported in order to distinguish the contribution of this single salt bridge in the initial steps of amyloid formation. Consequently, we decided to investigate the role of this salt bridge in early conformational rearrangements. To remove the salt bridge without perturbations in the backbone structure, the neutralized states of the involved residues were used. Three 10-ns molecular dynamics simulations on three initial structures have been performed. The results revealed that the early stages of the conformational rearrangements, against common belief, are mainly associated with the mutation-induced global changes in the backbone dynamics but not with the breaking of the salt bridge.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Bamdad K,Naderi-Manesh H

doi

10.1016/j.bbrc.2007.10.011

subject

Has Abstract

pub_date

2007-12-28 00:00:00

pages

719-24

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(07)02141-9

journal_volume

364

pub_type

杂志文章

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