NR ACDX
AU Callebaut,I.; Tasso,A.; Brasseur,R.; Burny,A.; Portetelle,D.; Mornon,J.P.
TI Common prevalence of alanine and glycine in mobile reactive centre loops of serpins and viral fusion peptides: do prions possess a fusion peptide?
QU Journal of Computer-Aided Molecular Design 1994 Apr; 8(2): 175-91
PT journal article
AB 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.
MH *Alanine; Amino Acid Sequence; Amino Acids/analysis; *Binding Sites; Comparative Study; Databases, Factual; *Glycine; Human; Models, Molecular; Molecular Sequence Data; Ovalbumin/chemistry; Prions/*chemistry/*metabolism; *Protein Structure, Secondary; Sequence Homology, Amino Acid; Serpins/*chemistry; Support, Non-U.S. Gov't; Viral Fusion Proteins/*chemistry/metabolism
AD Departement des Macromolecules Biologiques, CNRS URA09, Universites P6 et P7, Paris, France.
SP englisch
PO Niederlande