title: Structure-activity relationships for mini atrial natriuretic peptide by proline-scanning mutagenesis and shortening of peptide backbone.
abstract: MiniANP is a synthetic pentadecapeptide analogue of atrial natriuretic polypeptide (ANP). We have used the proline-scanning mutagenesis and the analogue peptides with shorter backbones to characterize the turn-like conformation at residue 6-9 and an extended structure of Gly5-Gly6 as the receptor-bound structure of miniANP. A docking study of miniANP at the binding site of the type A natriuretic peptide receptor (NPR-A) supported the deduced conformation in the receptor-bound structure.
authors.affiliation: Suntory Institute for Bioorganic Research, Shimamoto, 618-8503, Mishima, Japan.
authors.forename: Kenji
authors.initials: K
authors.lastname: Sugase
authors.forename: Yoshiaki
authors.initials: Y
authors.lastname: Oyama
authors.forename: Katsuhiko
authors.initials: K
authors.lastname: Kitano
authors.forename: Hideo
authors.initials: H
authors.lastname: Akutsu
authors.forename: Masaji
authors.initials: M
authors.lastname: Ishiguro
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D009320:Atrial Natriuretic Factor / Q000737:chemistry* / Q000235:genetics / Q000494:pharmacology*; D016466:CHO Cells; D006224:Cricetinae; D008969:Molecular Sequence Data; D016296:Mutagenesis; D011392:Proline / Q000737:chemistry*
chemical_list: D009320:Atrial Natriuretic Factor; D011392:Proline