1hrl
From Proteopedia
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[[Image:1hrl.jpg|left|200px]] | [[Image:1hrl.jpg|left|200px]] | ||
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'''STRUCTURE OF A PARALYTIC PEPTIDE FROM AN INSECT, MANDUCA SEXTA''' | '''STRUCTURE OF A PARALYTIC PEPTIDE FROM AN INSECT, MANDUCA SEXTA''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HRL is a [[Single protein]] structure | + | 1HRL is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HRL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Prakash, O.]] | [[Category: Prakash, O.]] | ||
[[Category: Yu, X Q.]] | [[Category: Yu, X Q.]] | ||
| - | [[Category: | + | [[Category: Enf family]] |
| - | [[Category: | + | [[Category: Paralytic peptide]] |
| - | [[Category: | + | [[Category: Plasmatocyte spreading peptide]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:09:49 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 16:09, 2 May 2008
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. 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 Page seeded by OCA on Fri May 2 19:09:49 2008
