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Growth-blocking peptide (GBP) is an insect cytokine that possesses diverse biological activities such as lar-val growth regulation, cell proliferation, and stimula-tion of immune cells. GBP is a 25-amino acid peptide with one disulfide bond. It has been revealed that the tertiary structure of GBP consists of an N- and C- terminal disordered region and a well-structured core. Although there is only a slight similarity between the primary structures of GBP and EGF and the molecu-lar weight of GBP is about half that of EGF, GBP di-rectly binds and activates the EGF receptor of human keratinocyte cells. Furthermore, the tertiary structure of the well-defined region of GBP is similar to that of the C-terminal domain of EGF. This review will focus on the tertiary structure of GBP and its activities, as compared with those of EGF.