2EQQ

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

2EQQ の概要

• エントリーDOI: 10.2210/pdb2eqq/pdb
• 関連するPDBエントリー: 2EQH 2EQT
• 分子名称: Growth-blocking peptide, long form (1 entity in total)
• 機能のキーワード: growth-blocking peptide, cytokine
• 由来する生物種: Mythimna separata (northern armyworm)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3115.54

構造登録者

Umetsu, Y.,Aizawa, T.,Kamiya, M.,Kumaki, Y.,Demura, M.,Kawano, K. (登録日: 2007-03-30, 公開日: 2008-04-01, 最終更新日: 2024-10-16)

主引用文献

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

実験手法

SOLUTION NMR