1hrl
From Proteopedia
(New page: 200px<br /><applet load="1hrl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hrl" /> '''STRUCTURE OF A PARALYTIC PEPTIDE FROM AN INS...) |
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- | [[Image:1hrl.jpg|left|200px]]<br /><applet load="1hrl" size=" | + | [[Image:1hrl.jpg|left|200px]]<br /><applet load="1hrl" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1hrl" /> | caption="1hrl" /> | ||
'''STRUCTURE OF A PARALYTIC PEPTIDE FROM AN INSECT, MANDUCA SEXTA'''<br /> | '''STRUCTURE OF A PARALYTIC PEPTIDE FROM AN INSECT, MANDUCA SEXTA'''<br /> | ||
==Overview== | ==Overview== | ||
- | Paralytic peptide 1 (PP1) from a moth, Manduca sexta, is a 23-residue | + | 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== | ==About this Structure== | ||
- | 1HRL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 1HRL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HRL OCA]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10517164 10517164] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10517164 10517164] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
- | [[Category: Kanost, M | + | [[Category: Kanost, M R.]] |
[[Category: Prakash, O.]] | [[Category: Prakash, O.]] | ||
- | [[Category: Yu, X | + | [[Category: Yu, X Q.]] |
[[Category: enf family]] | [[Category: enf family]] | ||
[[Category: paralytic peptide]] | [[Category: paralytic peptide]] | ||
[[Category: plasmatocyte spreading peptide]] | [[Category: plasmatocyte spreading peptide]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:04:09 2008'' |
Revision as of 11:04, 21 February 2008
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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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