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. Author manuscript; available in PMC: 2017 Nov 1.
Published in final edited form as: Biochim Biophys Acta. 2016 Jun 3;1860(11 Pt B):2672–2681. doi: 10.1016/j.bbagen.2016.05.040

Table 3.

Summary of the complex structure of prion-antibodies

code antigen antibody epitope refs

2w9e huPrP (119–231) ICSM 18 Fab (H1, 143–156) [63]

1tpx OvPrPC and OvPrPSC VRQ14 Fab 188–199 [64]
(114–234)
1. A136-R154-R171
2. V136-R154-Q171
3. A136-R154-Q171

4DGI huPrPc (120–230) POM1 Fab Primary: (residues 140–147) [65]
Secondary: Lys204, Arg208 and Gln212

4YX2 boPrP(103–242), POM1 Fab The same with huPrP [66]
4YXH dePrP (123–231),
4YXK ekPrP (124–231) ,
4YXL shPrP (90–230)

4j8r Peptide OR2 POM2 Fab PHGGSWGQPHGGSWGQ [62]
PHGGSWGQPHGGS WGQ

1cr9 peptide epitope (SHaPrP 104–113) 3F4 Fab KPKTNMKHMA [61]

4kml full-length HuPrP nanobody (Nb484) discontinuous epitope including residues [67]
123–125 in the β0-β1 loop, residues 164–170 in the β2-α2
loop, and residues
174–185 in the α2-helix.