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Article

NMR structures of three single-residue variants of the human prion protein.

Proceedings of the National Academy of Sciences of the United States of America - 18 Jul 2000

Calzolai L, Lysek D A, Guntert P, von Schroetter C, Riek R, Zahn R, Wüthrich K

Abstract excerpt

The NMR structures of three single-amino acid variants of the C-terminal domain of the human prion protein, hPrP(121-230), are presented. In hPrP(M166V) and hPrP(R220K) the substitution is with the corresponding residue in murine PrP, and in hPrP(S170N) it is with the corresponding Syrian hamster residue. All three substitutions are in the surface region of the structure of the cellular form of PrP (PrP(C)) that...

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Identifiers

PMID: 10900000
DOI: 10.1073/pnas.97.15.8340
PMCID: PMC26949

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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