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Article

NMR structure of a variant human prion protein with two disulfide bridges.

Journal of molecular biology - 7 Feb 2003

Zahn Ralph, Güntert Peter, von Schroetter Christine, Wüthrich Kurt

Abstract excerpt

The nuclear magnetic resonance structure of the globular domain with residues 121-230 of a variant human prion protein with two disulfide bonds, hPrP(M166C/E221C), shows the same global fold as wild-type hPrP(121-230). It contains three alpha-helices of residues 144-154, 173-194 and 200-228, an anti-parallel beta-sheet of residues 128-131 and 161-164, and the disulfides Cys166-Cys221 and Cys179-Cys214. The...

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Identifiers

PMID: 12547204
DOI: 10.1016/s0022-2836(02)01332-3

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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