ANTISENSE HOMOLOGY BOXES IN PROTEINS

Lajos BARANYI[1]
William CAMPBELL[1]
Hidechika OKADA[2]

[1] Choju Medical Institute, Fukushimura Hospital
19-14 Aza Yamanaka. Toyohashi. 441 Japan
[2] Department of Molecular Biology Nagoya City University School of Medicine,
Nagoya 467, JAPAN


Abstract

Amphiphilic peptides approximately fifteen amino acids in length and their corresponding antisense peptides exist within protein molecules. These regions (termed antisense homology boxes) are separated by approximately fifty amino acids. Since many sense-antisense peptide pairs have been reported to recognize and bind to each other, antisense homology boxes may be involved in folding, chaperoning and oligomer formation of proteins. The finding that cc 70 per cent of the antisense homology box derived peptides from C5a receptor and human Endothelin A receptor are specific inhibitors or agonist to their corresponding proteins indicate that these regions can have significant role in proteins.