2jr8
From Proteopedia
Solution structure of Manduca sexta moricin
Overview
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 (1)H--(1)H -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. Copyright (c) 2008 European Peptide Society and John Wiley & Sons, Ltd.
About this Structure
2JR8 is a Single protein structure. Full crystallographic information is available from OCA.
Reference
Solution structure, antibacterial activity, and expression profile of Manduca sexta moricin., Dai H, Rayaprolu S, Gong Y, Huang R, Prakash O, Jiang H, J Pept Sci. 2008 Feb 11;. PMID:18265434 Page seeded by OCA on Sun May 4 09:12:48 2008
