1hrl: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| (10 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==STRUCTURE OF A PARALYTIC PEPTIDE FROM AN INSECT, MANDUCA SEXTA== | |||
<StructureSection load='1hrl' size='340' side='right'caption='[[1hrl]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1hrl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Manduca_sexta Manduca sexta]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HRL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HRL FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hrl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hrl OCA], [https://pdbe.org/1hrl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hrl RCSB], [https://www.ebi.ac.uk/pdbsum/1hrl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hrl ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PAP1_MANSE PAP1_MANSE] Causes rapid, rigid paralysis when injected into Lepidopteran larvae. The physiological role may be to reduce hemolymph loss following injury and promote wound healing. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
== | |||
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. | ||
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<ref>PMID:10517164</ref> | |||
Structure of a paralytic peptide from an insect, Manduca sexta., Yu XQ, Prakash O, Kanost MR | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1hrl" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Manduca sexta]] | |||
[[Category: Kanost MR]] | |||
[[Category: Prakash O]] | |||
[[Category: Yu X-Q]] | |||
Latest revision as of 07:15, 10 May 2023
STRUCTURE OF A PARALYTIC PEPTIDE FROM AN INSECT, MANDUCA SEXTA
| ||||||||||||
