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Solution structure of an insect growth factor, growth-blocking peptide
T Aizawa1, N Fujitani, Y Hayakawa
1Division of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo 060-0810, Japan.
The Journal of Biological Chemistry
|January 16, 1999
Summary
Growth-blocking peptide (GBP), an insect growth factor, has its first 3D structure revealed. This structure is similar to epidermal growth factor (EGF), suggesting potential interactions with the EGF receptor.
Area of Science:
- Structural biology
- Peptide science
- Insect physiology
Background:
- Growth-blocking peptide (GBP) is a 25-amino acid insect growth factor.
- GBP exhibits dose-dependent effects, retarding lepidopteran larval development at high concentrations and stimulating growth at low concentrations.
Purpose of the Study:
- To determine the three-dimensional solution structure of Growth-blocking peptide (GBP).
- To investigate the structural relationship between GBP and other growth factors.
Main Methods:
- Two-dimensional 1H NMR spectroscopy was employed to determine the solution structure of GBP.
- Analysis of secondary structure elements including beta-sheets and beta-turns.
Main Results:
- The determined structure of GBP reveals a short double-stranded beta-sheet (residues 11-13 and 19-21) and a type-II beta-turn (residues 8-11).
- The N and C termini of GBP were found to be disordered.
- The well-defined region of GBP shares structural similarity with the C-terminal domain of epidermal growth factor (EGF).
Conclusions:
- This is the first reported 3D structure of a peptiderigic insect growth factor.
- The structural similarity between GBP and EGF suggests a potential interaction of GBP with the EGF receptor, given GBP's reported ability to stimulate DNA synthesis in both insect and human cells.