1HRL
STRUCTURE OF A PARALYTIC PEPTIDE FROM AN INSECT, MANDUCA SEXTA
Summary for 1HRL
| Entry DOI | 10.2210/pdb1hrl/pdb |
| Descriptor | PARALYTIC PEPTIDE I (1 entity in total) |
| Functional Keywords | paralytic peptide, plasmatocyte spreading peptide, enf family, toxin |
| Total number of polymer chains | 1 |
| Total formula weight | 2438.72 |
| Authors | Yu, X.-Q.,Prakash, O.,Kanost, M.R. (deposition date: 2000-12-21, release date: 2001-01-10, Last modification date: 2017-12-20) |
| Primary citation | Yu, X.Q.,Prakash, O.,Kanost, M.R. Structure of a paralytic peptide from an insect, Manduca sexta. J.Pept.Res., 54:256-261, 1999 Cited by PubMed Abstract: 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. PubMed: 10517164DOI: 10.1034/j.1399-3011.1999.00136.x PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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