1hrl

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STRUCTURE OF A PARALYTIC PEPTIDE FROM AN INSECT, MANDUCA SEXTA

Overview

Paralytic peptide 1 (PP1) from a moth, Manduca sexta, is a 23-residue, peptide, (Glu-Asn-Phe-Ala-Gly-Gly-Cys-Ala-Thr-Gly-Tyr-Leu-Arg-Thr-Ala-Asp-Gly-Arg, -Cys-Lys-Pro-Thr-Phe) that was first found to have paralytic activity when, injected into M. sexta larvae. Recent studies demonstrated that PP1 also, stimulated the spreading and aggregation of a blood cell type called, plasmatocytes and inhibited bleeding from wounds. We determined the, solution structure of PP1 by two-dimensional 1H NMR spectroscopy to begin, to understand structural-functional relationships of this peptide. PP1 has, an ordered structure, which is composed of a short antiparallel beta-sheet, at residues Tyr11-Thr14 and Arg18-Pro21, three beta turns at residues, Phe3-Gly6, Ala8-Tyr11 and Thr14-Gly17, and a half turn at the, carboxyl-terminus (residues Lys20-Phe23). The well-defined secondary and, tertiary structure was stabilized by hydrogen bonding and side-chain, hydrophobic interactions. In comparison with two related insect peptides, whose structures have been solved recently, the amino-terminal region of, PP1 is substantially more ordered. The short antiparallel beta-sheet of, PP1 has a folding pattern similar to the carboxyl-terminal subdomain of, epidermal growth factor (EGF). Therefore, PP1 may interact with EGF, receptor-like molecules to trigger its different biological activities.

About this Structure

1HRL is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.

Reference

Structure of a paralytic peptide from an insect, Manduca sexta., Yu XQ, Prakash O, Kanost MR, J Pept Res. 1999 Sep;54(3):256-61. PMID:10517164

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