2JR8

Solution structure of Manduca sexta moricin

2JR8 の概要

• エントリーDOI: 10.2210/pdb2jr8/pdb
• NMR情報: BMRB: 15323
• 分子名称: Antimicrobial peptide moricin (1 entity in total)
• 機能のキーワード: antimicrobial peptide, antimicrobial protein
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4551.54

構造登録者

Gong, Y.,Dai, H.,Rayaprolu, S.,Huang, R.,Prakash, O.,Jiang, H. (登録日: 2007-06-21, 公開日: 2008-03-25, 最終更新日: 2024-05-08)

主引用文献

Dai, H.,Rayaprolu, S.,Gong, Y.,Huang, R.,Prakash, O.,Jiang, H.
Solution structure, antibacterial activity, and expression profile of Manduca sexta moricin.
J.Pept.Sci., 14:855-863, 2008

PubMed Abstract: In response to wounding or infection, insects produce a battery of antimicrobial peptides (AMPs) and other defense molecules to kill the invading pathogens. To study their structures, functions, and transcriptional regulation, we synthesized Manduca sexta moricin, a 42-residue peptide (GKIPVKAIKQAGKVIGKGLRAINIAGTTHDVVSFFRPKKKKH, 4539 Da). The compound exhibited potent antimicrobial activities against a broad spectrum of Gram-positive and Gram-negative bacteria with a minimum inhibitory concentration of 1.4 microM. The mRNA levels of M. sexta moricin increased substantially in fat body and hemocytes after the larvae were challenged with bacterial cells. We determined the solution structure of this AMP by two-dimensional 1H-1H -nuclear magnetic resonance spectroscopy. The tertiary structure is composed of an eight-turn alpha-helix spanning almost the entire peptide. Insights of relationships between the structure and function are also presented.

PubMed: 18265434
DOI: 10.1002/psc.1016

実験手法

SOLUTION NMR