NR AIOY
AU Mornon,J.P.; Prat,K.; Dupuis,F.; Callebaut,I.
TI Structural features of prions explored by sequence analysis I. Sequence data.
QU Cellular and Molecular Life Science 2002 Aug; 59(8): 1366-76
PT journal article
AB Animal prion proteins (PrPs) form at the sequence level a very homogenous and 'closed' family. Therefore, few of their structural and functional features can be gleaned from sequence comparison as is now possible on a wide scale for other protein families. To detect putatively related proteins (at the structural and/or functional level), we used a battery of sequence analysis tools. This analysis resulted in (i) the identification of a putative 'prion-like' domain within the envelope of foamy retroviruses, (ii) the detection of putative similarities between prions and an interferon-inducible membrane protein, and (iii) the proposal that of the TATA-box-binding protein is a structural scaffold, which might allow understanding of a key event leading to the structural conversion from PrPc (normal cellular prion structure) towards PrPsc (pathogenic structure).
MH Amino Acid Sequence; Animal; DNA-Binding Proteins/genetics; Human; Interferons/metabolism; Membrane Proteins/genetics; Molecular Sequence Data; Prions/*chemistry/genetics; Protein Structure, Tertiary; Sequence Alignment; Sequence Analysis, Protein; Spumavirus/chemistry/genetics; TATA-Box Binding Protein; Transcription Factors/genetics
AD Systemes Moleculaires & Biologie Structurale, LMCP, CNRS UMR 7590, Universites Paris 6 et Paris 7, France. mornon@lmcp.jussieu.fr
SP englisch
PO Schweiz