ISSN:
1573-4951
Keywords:
Serpin
;
Fusion
;
Envelope
;
Prion
;
Hydrophobic cluster analysis
;
Amino acid
;
Mobility
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Summary 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 spongi-form encephalopathies and resembling virus envelope proteins. These properties may be related to the infection mechanisms of these diseases.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00119866
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