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| Reference : Common Prevalence Of Alanine And Glycine In Mobile Reactive Center Loops Of Serpins And ... |
| Scientific journals : Article | |||
| Life sciences : Animal production & animal husbandry | |||
| http://hdl.handle.net/2268/33397 | |||
| Common Prevalence Of Alanine And Glycine In Mobile Reactive Center Loops Of Serpins And Viral Fusion Peptides - Do Prions Possess A Fusion Peptide | |
| English | |
| Callebaut, I. [> > > >] | |
| Tasso, A. [> > > >] | |
Brasseur, Robert  [Université de Liège > > Gembloux Agro-Bio Tech >] | |
| Burny, A. [> > > >] | |
| Portetelle, Daniel [Université de Liège > > Gembloux Agro-Bio Tech >] | |
| Mornon, Jp. [> > > >] | |
| 1994 | |
| Journal of Computer-Aided Molecular Design | |
| 8 | |
| 2 | |
| Yes (verified by ORBi) | |
| International | |
| 0920-654X | |
| [en] Serpin reactive centre loops and fusion peptides released by proteolytic cleavage
are particularly mobile. Their amino acid compositions reveal a common and unusual abundance of alanine, accompanied by high levels of glycine. These two small residues, which are not simultaneously abundant in stable helices (standard or transmembrane), probably play an important role in mobility. Threonine and valine (also relatively small amino acids) are also abundant in these two kinds of peptides. Moreover, the known 3D structures of an uncleaved serpin reactive centre and a fusion peptide are strikingly similar. Such sequences possess many small residues and are found in several signal peptides and in PrP, a protein associated with spongiform encephalopathies and resembling virus envelope proteins. These properties may be related to the infection mechanisms of these diseases. | |
| http://hdl.handle.net/2268/33397 | |
| also: http://hdl.handle.net/2268/108418 |
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