1hrl

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(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...)
Line 1: Line 1:
-
[[Image:1hrl.jpg|left|200px]]<br /><applet load="1hrl" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[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, 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.
+
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HRL OCA].
+
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.R.]]
+
[[Category: Kanost, M R.]]
[[Category: Prakash, O.]]
[[Category: Prakash, O.]]
-
[[Category: Yu, X.Q.]]
+
[[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://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:47:02 2007''
+
''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


1hrl

Drag the structure with the mouse to rotate

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

Page seeded by OCA on Thu Feb 21 13:04:09 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools