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. 2015 Jul 28;9(4):266–277. doi: 10.1080/19336896.2015.1065373

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© 2015 The Author(s). Published with license by Taylor & Francis Group, LLC

© Per Hammarström and Sofie Nyström

This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License http://creativecommons.org/licenses/by-nc/3.0/, which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.

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FIGURE 5. — Model of APrP fibrillar structure displayed as 8 in register parallel beta-sheet conformations as suggested by Groveman et al 2014 based on hamster PrP 90–231.⁴¹ Glycosylations (complex glycans) were added in silico using GlyProt.⁵⁴ Both N197 and N181 were distinguished as putative glycosylation sites by GlyProt. However, N181 was only accessible for glycosylations for one PrP chain at the end of the “elongating fibril” as shown in the back side of the model. N197 was accessible for glycosylation in all 8 PrP chains. Glycans are indicated in orange. Amino acid positions unique for PoPrP relative to HuPrP and BoPrP (Fig. 2b) are indicated in pink.