Prion protein description

This section starts with a detailed description of the globular domain in mPrP, which is the first prion protein for which a three-dimensional structure was obtained (Riek et al, 1996). Considering the high homology on the levels of both sequence (Fig. 1) and three-dimensional architecture (Fig. 8), the description of the proteins from the other three species concentrates on the structural differences relative to mPrP, and on data that were collected only for individual species. 

Pathological conditions are also linked to posttranslational modifications such as oxidized histidine residues found in P-amyloid protein of Alzheimer s patients, or conformational variants in the case of prion-induced encephalopathies. The development of sensitive MS tools and proteomics techniques is playing an active role in the precise description of these mechanisms.97,98... 

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