View source for 6oqp


==U-AITx-Ate1==
<StructureSection load='6oqp' size='340' side='right'caption='[[6oqp]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6oqp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinia_tenebrosa Actinia tenebrosa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OQP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OQP FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=6oqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oqp OCA], [https://pdbe.org/6oqp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6oqp RCSB], [https://www.ebi.ac.uk/pdbsum/6oqp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6oqp ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Sea anemone venoms have long been recognised as a rich source of peptides with interesting pharmacological and structural properties. Our recent transcriptomic studies of the Australian sea anemone Actinia tenebrosa have identified a novel 13-residue peptide, U-AITx-Ate1. U-AITx-Ate1 contains a single disulfide bridge and bears no significant homology to previously reported amino acid sequences of peptides from sea anemones or other species. We have produced U-AITx-Ate1 using solid-phase peptide synthesis, followed by oxidative folding and purification of the folded peptide using reversed-phase high-performance liquid chromatography. The solution structure of U-AITx-Ate1 was determined based on two-dimensional nuclear magnetic resonance spectroscopic data. Diffusion-ordered NMR spectroscopy revealed that U-AITx-Ate1 was monomeric in solution. Perturbations in the 1D (1)H NMR spectrum of U-AITx-Ate1 in the presence of dodecylphosphocholine micelles together with molecular dynamics simulations indicated an interaction of U-AITx-Ate1 with lipid membranes, although no binding was detected to 100% POPC and 80% POPC: 20% POPG lipid nanodiscs by isothermal titration calorimetry. Functional assays were performed to explore the biological activity profile of U-AITx-Ate1. U-AITx-Ate1 showed no activity in voltage-clamp electrophysiology assays and no change in behaviour and mortality rates in crustacea. Moderate cytotoxic activity was observed against two breast cancer cell lines.

Structural and functional characterisation of a novel peptide from the Australian sea anemone Actinia tenebrosa.,Elnahriry KA, Wai DCC, Krishnarjuna B, Badawy NN, Chittoor B, MacRaild CA, Williams-Noonan BJ, Surm JM, Chalmers DK, Zhang AH, Peigneur S, Mobli M, Tytgat J, Prentis P, Norton RS Toxicon. 2019 Jul 11;168:104-112. doi: 10.1016/j.toxicon.2019.07.002. PMID:31302115<ref>PMID:31302115</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Actinia tenebrosa]]
[[Category: Large Structures]]
[[Category: Elnahriry KA]]
[[Category: Norton RS]]
[[Category: Wai DCC]]