View source for 5ngn


==Lybatide 2, a cystine-rich peptide from Lycium barbarum==
<StructureSection load='5ngn' size='340' side='right'caption='[[5ngn]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ngn]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Lycium_barbarum Lycium barbarum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NGN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NGN 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]] 1.48&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CCN:ACETONITRILE'>CCN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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=5ngn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ngn OCA], [https://pdbe.org/5ngn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ngn RCSB], [https://www.ebi.ac.uk/pdbsum/5ngn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ngn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A2D0TC93_LYCBA A0A2D0TC93_LYCBA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cysteine-rich peptides (CRPs) of 2-6 kDa are generally thermally and proteolytically stable because of their multiple cross-bracing disulfide bonds. Here, we report the discovery and characterization of two novel cystine-stapled CRPs, designated lybatide 1 and 2 (lyba1 and lyba2), from the cortex of Lycium barbarum root. Lybatides, 32 to 33 amino acids in length, are hyperstable and display a novel disulfide connectivity with a cysteine motif of C-C-C-C-CC-CC which contains two pairs of adjacent cysteines (-CC-CC). X-ray structure analysis revealed the presence of a single cystine-stabilized (alpha + pi)-helix in lyba2, a rare feature of CRPs. Together, our results suggest that lybatides, one of the smallest four-disulfide-constrained plant CRPs, is a new family of CRPs. Additionally, this study provides new insights into the molecular diversity of plant cysteine-rich peptides and the unusual lybatide scaffold could be developed as a useful template for peptide engineering and therapeutic development.

Lybatides from Lycium barbarum Contain An Unusual Cystine-stapled Helical Peptide Scaffold.,Tan WL, Wong KH, Lei J, Sakai N, Tan HW, Hilgenfeld R, Tam JP Sci Rep. 2017 Jul 12;7(1):5194. doi: 10.1038/s41598-017-05037-1. PMID:28701689<ref>PMID:28701689</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5ngn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Lycium barbarum]]
[[Category: Hilgenfeld R]]
[[Category: Lei J]]
[[Category: Sakai N]]
[[Category: Tan WL]]