Copper and the prion protein: Function and dysfunction | Zendy

John H. Viles | Zendy

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Copper and the prion protein: Function and dysfunction

Author(s) -

John H. Viles

Publication year - 2005

Publication title -

the biochemist

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.126

H-Index - 7

eISSN - 1740-1194

pISSN - 0954-982X

DOI - 10.1042/bio02704009

Subject(s) - prion protein , infectivity , copper , microbiology and biotechnology , function (biology) , homeostasis , chemistry , biology , biophysics , biochemistry , virology , virus , medicine , pathology , disease , organic chemistry

The prion protein (PrP) has the ability to infect a host, and that infectivity is conferred by its conformation. The concept of an infectious protein presents a fascinating subject for those interested in protein structure. Cu2+ binds to a region of PrP vital for prion propagation, suggesting that the misfolding and fibrillization of PrP may be profoundly influenced by the presence of Cu2+ ions. The normal function of the prion protein has yet to be established, but its affinity for Cu2+ also suggests a role in copper homoeostasis.

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