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. Author manuscript; available in PMC: 2019 Nov 1.
Published in final edited form as: Neurobiol Dis. 2018 Jul 24;119:1–12. doi: 10.1016/j.nbd.2018.07.011

Figure 2. S174 stabilizes helix 2 in rabbit PrP.

Figure 2.

A and B, Detail of the NMR structure of HaPrP showing the position of N171 and N174 at the start of helix 2. N171 is right outside of helix 2. The β2-α2 loop is has an open conformation as indicated by the position of V166 and D167. C and D, Detail of the NMR structure of RaPrP-S174 showing the helix-capping domain formed by the aligned SI74 and N171. N171 is now included in the extended helix 2. The β2-α2 loop is now closer to helix 3 than in HaPrP as indicated by the position of V166 and D167. E and F, Detail of the NMR structure of RaPrP-S174N lacking the helix-capping domain. N171 is still included in the expanded helix 2 and the β2-α2 loop maintains its proximity to helix 3.