Structural features of prions explored by sequence analysis I. Sequence data.
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 PrP(C) (normal cellular prion structure) towards PrP(Sc) (pathogenic structure).
D000595:Amino Acid Sequence; D000818:Animals; D004268:DNA-Binding Proteins / Q000235:genetics; D058851:GPI-Linked Proteins; D006801:Humans; D007372:Interferons / Q000378:metabolism; D008565:Membrane Proteins / Q000235:genetics; D008969:Molecular Sequence Data; D011328:Prions / Q000737:chemistry* / Q000235:genetics; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D020539:Sequence Analysis, Protein; D016092:Spumavirus / Q000737:chemistry / Q000235:genetics; D035181:TATA-Box Binding Protein; D014157:Transcription Factors / Q000235:genetics
D004268:DNA-Binding Proteins; D058851:GPI-Linked Proteins; D008565:Membrane Proteins; C501125:PRND protein, human; D011328:Prions; D035181:TATA-Box Binding Protein; D014157:Transcription Factors; D007372:Interferons