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J Biol Chem, Vol. 274, Issue 4, 1887-1890, January 22, 1999

COMMUNICATION
Solution Structure of an Insect Growth Factor, Growth-blocking Peptide

Tomoyasu Aizawa, Naoki Fujitani, Yoichi Hayakawa^§, Atsushi Ohnishi^§, Tadayasu Ohkubo^¶, Yasuhiro Kumaki, Keiichi Kawano, Kunio Hikichi, and Katsutoshi Nitta

From the  Division of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo 060-0810, Japan, the ^§ Institute of Low Temperature Science, Hokkaido University, Sapporo 060-0819, Japan, the ^¶ Japan Advanced Institute of Science and Technology, Ishikawa 923-1292, Japan, and the  Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University, Toyama 930-0194, Japan

Growth-blocking peptide (GBP) is an insect growth factor consisting of 25 amino acid residues that retards the development of lepidopteran larvae at high concentration while it stimulates larval growth at low concentration. In this study, we determined the solution structure of GBP by two-dimensional ¹H NMR spectroscopy. The structure contains a short segment of double-stranded -sheet involving residues 11-13 and 19-21 and a type-II -turn in the loop region (residues 8-11), whereas the N and C termini are disordered. This is the first report of the three-dimensional structure of the peptiderigic insect growth factor, and the structure of the well defined region of GBP was found to share similarity with that of the C-terminal domain of the epidermal growth factor (EGF). Because GBP has been reported to stimulate DNA synthesis of not only insect cells but also human keratinocyte cells at the same level with EGF, the structural similarity between GBP and EGF may lead to the interaction of GBP to EGF receptor.

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Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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