2JOM

NMR structure of rabbit prion protein mutation I214V

Summary for 2JOM

• Entry DOI: 10.2210/pdb2jom/pdb
• NMR Information: BMRB: 15399
• Descriptor: Major prion protein (1 entity in total)
• Functional Keywords: prion protein, unknown function
• Biological source: Oryctolagus cuniculus (rabbit)
• Cellular location: Cell membrane; Lipid-anchor, GPI-anchor: Q95211
• Total number of polymer chains: 1
• Total formula weight: 16983.91

Authors

Li, J.,Lin, D. (deposition date: 2007-03-14, release date: 2008-01-29, Last modification date: 2023-12-20)

Primary citation

Wen, Y.,Li, J.,Xiong, M.,Peng, Y.,Yao, W.,Hong, J.,Lin, D.
Solution Structure and Dynamics of the I214V Mutant of the Rabbit Prion Protein.
Plos One, 5:e13273-e13273, 2010

PubMed Abstract: The conformational conversion of the host-derived cellular prion protein (PrP(C)) into the disease-associated scrapie isoform (PrP(Sc)) is responsible for the pathogenesis of transmissible spongiform encephalopathies (TSEs). Various single-point mutations in PrP(C)s could cause structural changes and thereby distinctly influence the conformational conversion. Elucidation of the differences between the wild-type rabbit PrP(C) (RaPrP(C)) and various mutants would be of great help to understand the ability of RaPrP(C) to be resistant to TSE agents.

PubMed: 20949107
DOI: 10.1371/journal.pone.0013273

Experimental method

SOLUTION NMR