Determinants of potency and temperature-dependent function in the Aplysia bag cell peptides.
Structure-activity relationships were determined for the natural bag cell peptides (BCPs) and for a series of synthetic analogues in terms of their ability to stimulate (at 30 degrees C) and to inhibit (at 15 degrees C) bag cell adenyl cyclase. We found that the core RLRF motif shared by all these peptides is active in this assay, and is stimulatory. The histidine residue C-terminal to this motif in beta-BCP is superfluous in this respect. An electronegative residue C-terminal to RLRF is sufficient to induce temperature-dependent function. The Ala-Pro pair that is N-terminal to this motif in alpha-BCP increases potency, but does not alter function.
Berry
R W
RW
Department of Cell, Molecular and Structural Biology, Northwestern University, School of Medicine, Chicago, IL 60611.
Hanu
R
R
Redman
R S
RS
Kim
J J
JJ
D000067956:Adenylyl Cyclase Inhibitors; D000262:Adenylyl Cyclases / Q000819:agonists / Q000187:drug effects*; D000595:Amino Acid Sequence; D066298:In Vitro Techniques; D007447:Invertebrate Hormones / Q000737:chemistry* / Q000494:pharmacology; D008958:Models, Molecular; D008969:Molecular Sequence Data; D013329:Structure-Activity Relationship; D013696:Temperature
D000067956:Adenylyl Cyclase Inhibitors; D007447:Invertebrate Hormones; C026880:egg-laying hormone, Mollusca; D000262:Adenylyl Cyclases