Structure-activity relationships for mini atrial natriuretic peptide by proline-scanning mutagenesis and shortening of peptide backbone.
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.
Sugase
Kenji
K
Suntory Institute for Bioorganic Research, Shimamoto, 618-8503, Mishima, Japan.
Oyama
Yoshiaki
Y
Kitano
Katsuhiko
K
Akutsu
Hideo
H
Ishiguro
Masaji
M
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*
D009320:Atrial Natriuretic Factor; D011392:Proline