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PubMed · 12363039

Structural features of prions explored by sequence analysis I. Sequence data.

J P Mornon·K Prat·F Dupuis·I Callebaut
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Abstract

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).

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Amino Acid SequenceAnimalsDNA-Binding ProteinsGPI-Linked ProteinsHumansInterferonsMembrane ProteinsMolecular Sequence DataPrionsProtein Structure, TertiarySequence AlignmentSequence Analysis, ProteinSpumavirusTATA-Box Binding ProteinTranscription FactorsJournal Article

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J P Mornon, K Prat, F Dupuis, I Callebaut. 2002. Structural features of prions explored by sequence analysis I. Sequence data.. https://doi.org/10.1007/s00018-002-8514-7

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