3D Structure of Human Prion Protein
On this page, you can see a molecule of human prion protein. The disease-causing ability of prions is caused by changes in polypeptide shape, making knowing the structure of the protein and places where this structure is less rigidly defined, vitally important to understanding prions.
Reset this prion molecule to the original view.
Notice the 3 alpha helices (pinkish) and 2 beta strands (golden).
These amino acids (167-171) are a source of change in protein shape. This loop shows a slow exchange between multiple backbone configurations.
These last two turns of the second and third alpha helices are in equilibrium with unfolded forms.
Neither the amino terminus nor the carboxyl terminus show up in the Jmol, but both also exhibit flexibility in structure. The the N-terminus would attach at the blue amino acid, the C-terminus at the red amino acid.
1. Zahn R, Liu A, Luhrs T, Riek R, von Schroetter C, Garcia F, Billeter M, Calzolai L, Wider G, Wuthrich K. NMR solution structure of the human prion protein. PNAS 2000; 97 (1): 145-150. http://www.pnas.org/content/97/1/145.full.pdf+html. Accessed 2010 Feb 13.
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