The conformation of alpha-human atrial natriuretic polypeptide in solution.
The three-dimensional structure of alpha-human ANP in solution was determined through the combined use of nuclear magnetic resonance spectroscopy and distance geometry. The results are based on distance constraints determined by nuclear Overhauser effect measurements and one disulfide bond. The structure is as follows. Three separate regions, which are Ser1-Cys7, Arg11-Ile15, and Gln18-Tyr28 each have some ordered structure. The remaining parts in the sequences of Gly9-Gly10 and Gly16-Ala17 act as hinges. And the C-terminal part is folded back toward the cyclic moiety. The conformation of alpha-hANP reported here is expected to give a better understanding of the relationships between its biological activities and three-dimensional structure.
Kobayashi
Y
Y
Institute for Protein Research, Osaka University.
Ohkubo
T
T
Kyogoku
Y
Y
Koyama
S
S
Kobayashi
M
M
Go
N
N
D000595:Amino Acid Sequence; D009320:Atrial Natriuretic Factor; D003198:Computer Simulation; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010446:Peptide Fragments; D011487:Protein Conformation; D012996:Solutions
D010446:Peptide Fragments; D012996:Solutions; D009320:Atrial Natriuretic Factor