2jr8 | pdb_00002jr8

Solution structure of Manduca sexta moricin

spinqualitylabelsall models 2jr8, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2jr8 is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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