NR AGYA
AU Kuznetsov,I.B.; Morozov,P.S.; Matushkin,Y.G.
TI Prion proteins: evolution and preservation of secondary structure.
QU FEBS Letters 1997 Aug 4; 412(3): 429-32
PT journal article
AB Prions cause a variety of neurodegenerative disorders that seem to result from a conformational change in the prion protein (PrP). Thirty-two PrP sequences have been subjected to phylogenetic analysis followed by reconstruction of the most probable evolutionary spectrum of amino acid replacements. The replacement rates suggest that the protein does not seem to be very conservative, but in the course of evolution amino acids have only been substituted within the elements of the secondary structure by those with very similar physico-chemical properties. Analysis of the full spectrum of single-step amino acid substitutions in human PrP using secondary structure prediction algorithms shows an over-representation of substitutions that tend to destabilize alpha-helices.
ZR 15
MH Amino Acids/chemistry/genetics; Animal; Chemistry, Physical; *Evolution, Molecular; Human; Magnetic Resonance Spectroscopy; Mice; Peptide Fragments/chemistry/genetics; Prions/*chemistry/genetics; *Protein Structure, Secondary; Support, Non-U.S. Gov't
AD Igor B. Kuznetsov (kuznets@bionet.nsc.ru), Pavel S. Morozov, Yuri G. Matushkin, Laboratory of Molecular Evolution, Institute of Cytology and Genetics, Russian Academy of Sciences, Prospekt Lavrentieva 10, Novosibirsk 630090, Russia
SP englisch
PO Niederlande
OR Prion-Krankheiten 5