Abstract:
:The C-terminally truncated Y145Stop variant of prion protein (PrP23-144) has been linked to a heritable prionopathy in humans and is also capable of triggering a transmissible prion disease in mice. PrP23-144 can be converted from soluble monomeric form to amyloid under physiological conditions, providing an in vitro model for investigating the molecular basis of amyloid strains and cross-seeding barriers. Here, we use magic-angle spinning solid-state NMR to establish the sequential backbone and sidechain 13C and 15N chemical shift assignments for amyloid fibrils formed by the A117V and M129V mutants of human PrP23-144, which in the context of full length PrP in vivo are among the specific residues associated with development of Gerstmann-Straüssler-Scheinker disease. The chemical shift data are utilized to identify amino acids comprising the rigid amyloid core regions and to predict the protein secondary structures for human PrP23-144 A117V and M129V fibrils.
journal_name
Biomol NMR Assignjournal_title
Biomolecular NMR assignmentsauthors
Dao HH,Hlaing MZ,Ma Y,Surewicz K,Surewicz WK,Jaroniec CPdoi
10.1007/s12104-020-09981-4subject
Has Abstractpub_date
2020-10-29 00:00:00eissn
1874-2718issn
1874-270Xpii
10.1007/s12104-020-09981-4pub_type
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