NR ABIX
AU Billeter,M.; Riek,R.; Wider,G.; Hornemann,S.; Glockshuber,R.; Wüthrich,K.
TI Prion protein NMR structure and species barrier for prion diseases
QU Proceedings of the National Academy of Sciences of the United States of America 1997 Jul 8; 94(14): 7281-5
IA http://www.pnas.org/cgi/content/full/94/14/7281
PT journal article
AB The structural basis of species specificity of transmissible spongiform encephalopathies, such as bovine spongiform encephalopathy or "mad cow disease" and Creutzfeldt-Jakob disease in humans, has been investigated using the refined NMR structure of the C-terminal domain of the mouse prion protein with residues 121-231. A database search for mammalian prion proteins yielded 23 different sequences for the fragment 124-226, which display a high degree of sequence identity and show relevant amino acid substitutions in only 18 of the 103 positions. Except for a unique isolated negative surface charge in the bovine protein, the amino acid differences are clustered in three distinct regions of the three-dimensional structure of the cellular form of the prion protein. Two of these regions represent potential species-dependent surface recognition sites for protein-protein interactions, which have independently been implicated from in vitro and in vivo studies of prion protein transformation. The third region consists of a cluster of interior hydrophobic side chains that may affect prion protein transformation at later stages, after initial conformational changes in the cellular protein.
ZR 17 Zitate
MH Amino Acid Sequence; Animals; Cattle; Humans; Magnetic Resonance Spectroscopy; Mice; Molecular Sequence Data; Prion Diseases/*transmission; Prions/*chemistry; Protein Conformation; Research Support, Non-U.S. Gov't; Species Specificity
AD Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule, CH-8093 Zürich, Switzerland.
SP englisch
PO USA
OR Prion-Krankheiten 2