Studies of the Structure-Activity Relationships of Peptides and Proteins Involved in Growth and Development Based on Their Three-Dimensional Structures

Abstract

Peptides and proteins with similar amino acid sequences can have different biological functions. Knowledge of their three-dimensional molecular structures is critically important in identifying their functional determinants. In this review, I describe the results of our and other groups' structure-based functional characterization of insect insulin-like peptides, a crustacean hyperglycemic hormone-family peptide, a mammalian epidermal growth factor-family protein, and an intracellular signaling domain that recognizes proline-rich sequence.

Isolation of an insulin-like peptide from the Asian malaria mosquito, Anopheles stephensi, that acts as a steroidogenic gonadotropin across diverse mosquito taxa

“…Later, cDNA was cloned from B. mori and found to encode the canonical pre-propeptide, indicating a C chain that was cleaved post-translation from the bioactive ILP. Chemically synthesized forms of B. mori ILPs also were shown to activate ecdysteroid hormone production by prothoracic glands in silkworms or bind to a putative insulin receptor (Ishizaki and Suzuki, 1994; Büllesbach, 1999; Nagata, 2010; Mizoguchi and Okamoto, 2013; Smith et al, 2014; Gu et al, 2015). Subsequently, this information led to the identification of more than 30 ILP genes in this species (Aslam et al, 2011), but the extent of their functional significance has not been explored.…”