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2laq
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 2laq is ON HOLD Authors: Moehle, K., Freund, A., Robinson, J.A. Description: Solution structure of the Sex Peptide from Drosophila melanogaster) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Solution structure of the Sex Peptide from Drosophila melanogaster== | |
| + | <StructureSection load='2laq' size='340' side='right'caption='[[2laq]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2laq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LAQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LAQ FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene></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=2laq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2laq OCA], [https://pdbe.org/2laq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2laq RCSB], [https://www.ebi.ac.uk/pdbsum/2laq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2laq ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A70A_DROME A70A_DROME] Represses female sexual receptivity and stimulates oviposition.<ref>PMID:3135120</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The insect sex peptide (SP) elicits a variety of biological responses upon transfer to the mated female. SP contains 36 amino acids, including a tryptophan-rich N-terminal region, a central region containing five hydroxyproline (Hyp) residues, and a C-terminal region enclosed by a disulfide bridge. The solution structure of SP, studied here using NMR spectroscopy, includes a motif WPWN that adopts a type I beta-turn in the N-terminal Trp-rich region. This turn region is connected to the central Hyp-rich region, which adopts extended and/or PPII-like conformations. The C-terminal disulfide-bonded loop populates helical turns or nascent helical structure. Overall, the results reveal a rather flexible peptide that lacks a compact folded structure in solution. | ||
| - | + | NMR studies of the solution conformation of the sex peptide from Drosophila melanogaster.,Moehle K, Freund A, Kubli E, Robinson JA FEBS Lett. 2011 Apr 20;585(8):1197-202. Epub 2011 Mar 23. PMID:21439282<ref>PMID:21439282</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2laq" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Drosophila melanogaster]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Freund A]] | ||
| + | [[Category: Moehle K]] | ||
| + | [[Category: Robinson JA]] | ||
Current revision
Solution structure of the Sex Peptide from Drosophila melanogaster
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