View source for 9hpp


==Helical form of Citropin 1.3==
<StructureSection load='9hpp' size='340' side='right'caption='[[9hpp]], [[Resolution|resolution]] 1.56&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9hpp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ranoidea_citropa Ranoidea citropa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9HPP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9HPP FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.56&#8491;</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=9hpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9hpp OCA], [https://pdbe.org/9hpp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9hpp RCSB], [https://www.ebi.ac.uk/pdbsum/9hpp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9hpp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CT13_RANCI CT13_RANCI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Citropin 1.3 is an antimicrobial peptide secreted by the amphibian Litoria citropa (Southern bell frog). In this study, the structural and functional properties of its non-amidated form, which self-assembles into distinct fibrillar architectures, are investigated. Using cryogenic electron microscopy, X-ray crystallography, and fluorescence microscopy with model membranes and cells, diverse supramolecular structures, including canonical amyloid fibrils, multilayered nanotubes, and a novel mixed fibril type, are identified. In giant unilamellar vesicles, citropin 1.3 promoted membrane fusion and underwent lipid-induced phase separation. In mammalian cells, it permeabilized membranes, induced cell death, and colocalized with nucleic acids. These findings link antimicrobial activity to amyloid assembly and highlight the peptide's structural plasticity and potential biological functions, offering new insights into amyloid-based antimicrobial mechanisms.

Structural and Functional Versatility of the Amyloidogenic Non-Amidated Variant of the Antimicrobial Peptide Citropin 1.3.,Strati F, Cali MP, Bloch Y, Mostafavi S, Monistrol J, Golubev A, Rayan B, Gustavsson E, Landau M Adv Sci (Weinh). 2025 Sep 28:e03997. doi: 10.1002/advs.202503997. PMID:41016026<ref>PMID:41016026</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9hpp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Ranoidea citropa]]
[[Category: Bloch Y]]
[[Category: Landau M]]
[[Category: Rayan B]]