Abstract:
:The scrapie prion protein (PrPSc) is formed from the cellular isoform (PrPC) by a post-translational process that involves a profound conformational change. Linear epitopes for recombinant antibody Fab fragments (Fabs) on PrPC and on the protease-resistant core of PrPSc, designated PrP 27-30, were identified using ELISA and immunoprecipitation. An epitope region at the C terminus was accessible in both PrPC and PrP 27-30; in contrast, epitopes towards the N-terminal region (residues 90 to 120) were accessible in PrPC but largely cryptic in PrP 27-30. Denaturation of PrP 27-30 exposed the epitopes of the N-terminal domain. We argue from our findings that the major conformational change underlying PrPSc formation occurs within the N-terminal segment of PrP 27-30.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Peretz D,Williamson RA,Matsunaga Y,Serban H,Pinilla C,Bastidas RB,Rozenshteyn R,James TL,Houghten RA,Cohen FE,Prusiner SB,Burton DRdoi
10.1006/jmbi.1997.1328subject
Has Abstractpub_date
1997-10-31 00:00:00pages
614-22issue
3eissn
0022-2836issn
1089-8638pii
S0022-2836(97)91328-0journal_volume
273pub_type
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