The prion protein is a copper binding glycoprotein that in mammals can misfold into a pathogenic isoform leading to prion diseases, as opposed, surprisingly, to avians. The avian prion N-terminal tandem repeat is richer in prolines than the mammal one, and understanding their effect on conformation is of great biological importance. Here we succeeded in investigating the conformations of a single avian hexarepeat by means of NMR and Molecular Dynamics techniques. We found a high flexibility and a strong conformational dependence on pH: local turns are present at acidic and neutral pH, while unordered regions dominate at basic conditions.

An NMR and Molecular Dynamics investigation of the Avian Prion Hexarepeat conformational features in solution

PIETROPAOLO, ADRIANA;MUCCIOLI, LUCA;ZANNONI, CLAUDIO;
2007

Abstract

The prion protein is a copper binding glycoprotein that in mammals can misfold into a pathogenic isoform leading to prion diseases, as opposed, surprisingly, to avians. The avian prion N-terminal tandem repeat is richer in prolines than the mammal one, and understanding their effect on conformation is of great biological importance. Here we succeeded in investigating the conformations of a single avian hexarepeat by means of NMR and Molecular Dynamics techniques. We found a high flexibility and a strong conformational dependence on pH: local turns are present at acidic and neutral pH, while unordered regions dominate at basic conditions.
A. Pietropaolo; L. Raiola; L. Muccioli; G. Tiberio; C. Zannoni; R. Fattorusso; C. Isernia; D. La Mendola; G. Pappalardo; E. Rizzarelli
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11585/53358
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