NR AMSC
AU Wong,N.K.C.; Renouf,D.V.; Lehmann,S.; Hounsell,E.F.
TI Glycosylation of prions and its effects on protein conformation relevant to amino acid mutations
QU Journal of Molecular Graphics and Modelling 2000 Apr; 18(2): 126-34, 163-5
PT journal article
AB The three-dimensional coordinates from a nuclear magnetic resonance (NMR)-averaged structure containing residues 121-226 of mouse prion were used as the starting geometry for MD of prion either with or without glycan in both mutant and wild-type forms. The following mutants were studied: Asp-178 to Asn, Thr-183 to Ala, Phe-198 to Ser, Glu-200 to Lys, and Gln-217 to Arg. NMR data vs structural models were compared to observe any major differences. Simulations of the change in protein structure with and without glycan were performed, as they cannot be tested by NMR analysis. Several mutants were expressed and analyzed for altered glycosylation and the results interpreted in terms of molecular modeling. N-linked glycosylation is likely to play an important role in prion biology as shown by visualization of glycoprotein conformation.
MH Amino Acid Sequence; Amino Acid Substitution/*genetics; Animal; CHO Cells; Computer Simulation; Glycosylation; Hamsters; Hydrogen Bonding; Mice; Models, Molecular; Molecular Sequence Data; Mutation/*genetics; Nuclear Magnetic Resonance, Biomolecular; Polysaccharides/chemistry; Prions/*chemistry/*genetics/metabolism; Protein Conformation; Support, Non-U.S. Gov't; Thermodynamics; Trisaccharides/chemistry
AD School of Biological & Chemical Sciences, Birkbeck, University of London, United Kingdom. n.wong@sbc.bbk.ac.uk
SP englisch
PO USA