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1H, 13C, 15N backbone and side-chain resonance assignments of the pathogenic G131V mutant of human prion protein (91-231).

Biomolecular NMR assignments - 1 Oct 2021

Zhang Qiaodong, Zhang Haoran, Zheng Fengyu, Liu Rong, Liao Xinli, Guo Chenyun, Lin Donghai

Abstract excerpt

Human prion disease, also known as transmissible spongiform encephalopathy (TSEs), is caused by the conformational conversion of the normal cellular prion protein (PrPC) into the scrapie form (PrPSc). Pathogenic point mutations of prion proteins typically facilitate conformational conversion and lead to inherited prion diseases. A previous study has demonstrated that the pathogenic G131V mutation of human prion...

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PMID: 33871829
DOI: 10.1007/s12104-021-10022-x

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