The antisense homology box: A new motif within proteins that encodes biologically active peptides

Lajos Baranyi, William Campbell, Kunihiro Ohshima, Seigo Fujimoto, Mihäly Boros, Hidechika Okada

Research output: Contribution to journalArticle

97 Citations (Scopus)

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. Because 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 antisense homology box-derived peptide CALSVDRYRAVASW, a fragment of human endothelin A receptor, proved to be a specific inhibitor of endothelin peptide (ET-1) in a smooth muscle relaxation assay. The peptide was able to block endotoxin-induced shock in rats as well. Our finding of endothelin receptor inhibitor among antisense homology box-derived peptides indicates that searching proteins for this new motif may be useful in finding biologically active peptides.

Original languageEnglish
Pages (from-to)894-901
Number of pages8
JournalNature medicine
Volume1
Issue number9
DOIs
Publication statusPublished - Sep 1995

    Fingerprint

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this