View source for 5xdi


==Vaccatide: Antifungal Glutamine-rich 8C-Hevein-like Peptide, vH1==
<StructureSection load='5xdi' size='340' side='right'caption='[[5xdi]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5xdi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gypsophila_vaccaria Gypsophila vaccaria]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XDI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XDI 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=5xdi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xdi OCA], [https://pdbe.org/5xdi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xdi RCSB], [https://www.ebi.ac.uk/pdbsum/5xdi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xdi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A2D0TCI2_GYPVA A0A2D0TCI2_GYPVA] 
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== Publication Abstract from PubMed ==
Hevein and hevein-like peptides are disulfide-constrained chitin-binding cysteine-rich peptides. They are divided into three subfamilies, 6C-, 8C-, and 10C-hevein-like peptides, based on the number of cysteine residues. In addition, hevein-like peptides can exist in two forms, short and long. The long C-terminal form found in hevein and 10C-hevein-like peptides contain a C-terminal protein cargo. In contrast, the short form without a protein cargo is found in all three subfamilies. Here, we report the discovery and characterization of two novel glutamine-rich and protein cargo-free 8C-hevein-like peptides, vaccatides vH1 and vH2, from Vaccaria hispanica of the Caryophyllaceae family. Proteomic analyses showed that the vaccatides are 40-41 amino acids in length and contain a chitin-binding domain. NMR determination revealed that vaccatide vH2 displays a highly compact structure with a N-terminal cystine knot and an addition C-terminal disulfide bond. Stability studies showed that this compact structure renders vaccatide vH2 resistant to thermal, chemical and proteolytic degradation. The chitin-binding vH2 was shown to inhibit the mycelium growth of four phyto-pathogenic fungal strains with IC50 values in the micromolar range. Our findings show that vaccatides represent a new family of 8C-hevein-like peptides, which are protein cargo-free and glutamine-rich, characteristics that differentiate them from the prototypic hevein and the 10C-hevein-like peptides. In summary, this study enriches the existing library of hevein-like peptides and provides insight into their molecular diversity in sequence, structure and biosynthesis. Additionally, their highly disulfide-constrained structure could be used as a scaffold for developing metabolically and orally active peptidyl therapeutics.

Vaccatides: Antifungal Glutamine-Rich Hevein-Like Peptides from Vaccaria hispanica.,Wong KH, Tan WL, Kini SG, Xiao T, Serra A, Sze SK, Tam JP Front Plant Sci. 2017 Jun 21;8:1100. doi: 10.3389/fpls.2017.01100. eCollection, 2017. PMID:28680440<ref>PMID:28680440</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gypsophila vaccaria]]
[[Category: Large Structures]]
[[Category: Tam JP]]
[[Category: Xiao T]]