Prediction of the biologically active sites in eclosion hormone from the silkworm, Bombyx mori.
The structure-activity relationship of eclosion hormone from the silkworm, Bombyx mori, was analyzed. First, the probable active residues in silkworm eclosion hormone and also tobacco hornworm eclosion hormone were predicted by the average distance map method. To examine the contributions of those residues to the activity of silkworm eclosion hormone, Gly-substituted mutants for those predicted residues were produced by site-directed mutagenesis and their activities were evaluated by a bioassay. Finally, Glu12, Met24 and Phe25 were estimated to be the crucial residues for the eclosion hormone activity. The possibility of the development of a blocker of an eclosion hormone receptor on the basis of the present work is also discussed.
Kikuchi
T
T
International Research Laboratories, Ciba-Geigy Ltd., Takarazuka, Japan.
Okamoto
M
M
Geiser
M
M
Schmitz
A
A
Gohda
K
K
Takai
M
M
Morita
T
T
Horii
K
K
Fujita
N
N
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D012831:Bombyx; D004926:Escherichia coli; D007301:Insect Hormones / Q000737:chemistry* / Q000235:genetics; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D017433:Protein Structure, Secondary; D013329:Structure-Activity Relationship
D007301:Insect Hormones; C042645:eclosion hormone