2EQH

Solution structure of growth-blocking peptide of the armyworm, Pseudaletia separata

Summary for 2EQH

• Entry DOI: 10.2210/pdb2eqh/pdb
• Related: 2EQQ 2EQT
• Descriptor: Growth-blocking peptide, short form (1 entity in total)
• Functional Keywords: growth-blocking peptide, cytokine
• Biological source: Mythimna separata (northern armyworm)
• Total number of polymer chains: 1
• Total formula weight: 2496.82

Authors

Umetsu, Y.,Aizawa, T.,Kamiya, M.,Kumaki, Y.,Demura, M.,Kawano, K. (deposition date: 2007-03-30, release date: 2008-04-01, Last modification date: 2024-11-13)

Primary citation

Umetsu, Y.,Aizawa, T.,Muto, K.,Yamamoto, H.,Kamiya, M.,Kumaki, Y.,Mizuguchi, M.,Demura, M.,Hayakawa, Y.,Kawano, K.
C-terminal elongation of growth-blocking peptide enhances its biological activity and micelle binding affinity
J.Biol.Chem., 284:29625-29634, 2009

PubMed Abstract: Growth-blocking peptide (GBP) is a hormone-like peptide that suppresses the growth of the host armyworm. Although the 23-amino acid GBP (1-23 GBP) is expressed in nonparasitized armyworm plasma, the parasitization by wasp produces the 28-amino acid GBP (1-28 GBP) through an elongation of the C-terminal amino acid sequence. In this study, we characterized the GBP variants, which consist of various lengths of the C-terminal region, by comparing their biological activities and three-dimensional structures. The results of an injection study indicate that 1-28 GBP most strongly suppresses larval growth. NMR analysis shows that these peptides have basically the same tertiary structures and that the extension of the C-terminal region is disordered. However, the C-terminal region of 1-28 GBP undergoes a conformational transition from a random coiled state to an alpha-helical state in the presence of dodecylphosphocholine micelles. This suggests that binding of the C-terminal region would affect larval growth activity.

PubMed: 19710009
DOI: 10.1074/jbc.M109.011148

Experimental method

SOLUTION NMR