Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins.
Extensive regions of heptad repeat units consistent with an alpha-helical coiled coil conformation are located adjacent to hydrophobic, potentially fusion-related regions in the amino acid sequences of paramyxovirus fusion and retrovirus envelope glycoproteins. Similar arrangements of hydrophobic peptides and heptad repeat units exist in coronavirus peplomer proteins and influenza virus haemagglutinins. This suggests that there may be similarities in the structures of these proteins and in the functions of the hydrophobic fusion-related regions during virus entry.
Chambers
P
P
Department of Biological Sciences, University of Warwick, Coventry, U.K.
Pringle
C R
CR
Easton
A J
AJ
D000595:Amino Acid Sequence; D001358:Avian Sarcoma Viruses / Q000235:genetics; D003332:Coronaviridae / Q000235:genetics; D009980:Influenza A virus / Q000235:genetics; D008969:Molecular Sequence Data; D009522:Newcastle disease virus / Q000235:genetics; D011487:Protein Conformation; D012091:Repetitive Sequences, Nucleic Acid; D014760:Viral Fusion Proteins / Q000235:genetics*
D014760:Viral Fusion Proteins