View source for 5kkm


==Con-Vc11-22==
<StructureSection load='5kkm' size='340' side='right'caption='[[5kkm]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5kkm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Conus_victoriae Conus victoriae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KKM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KKM 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=5kkm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kkm OCA], [https://pdbe.org/5kkm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kkm RCSB], [https://www.ebi.ac.uk/pdbsum/5kkm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kkm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O2VC1_CONVC O2VC1_CONVC] Unknown. Intracranial injection of the peptide into mice does not produce toxic effects (PubMed:26774129). In addition, the peptide does not produce any observable changes to normal or depolarization-induced intracellular calcium levels in mouse dorsal root ganglion cells (PubMed:26774129).<ref>PMID:26774129</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Grafting bioactive peptide sequences onto small cysteine-rich scaffolds is a promising strategy for enhancing their stability and value as novel peptide-based therapeutics. However, correctly folded disulfide-rich peptides can be challenging to produce by either recombinant or synthetic means. The single disulfide-directed beta-hairpin (SDH) fold, first observed in contryphan-Vc1, provides a potential alternative to complex disulfide-rich scaffolds. We have undertaken recombinant production of full-length contryphan-Vc1 (rCon-Vc1[Z1Q]) and a truncated analogue (rCon-Vc11-22[Z1Q]), analyzed the backbone dynamics of rCon-Vc1[Z1Q], and probed the conformational and proteolytic stability of these peptides to evaluate the potential of contryphan-Vc1 as a molecular scaffold. Backbone 15N relaxation measurements for rCon-Vc1[Z1Q] indicate that the N-terminal domain of the peptide is ordered up to Thr19, whereas the remainder of the C-terminal region is highly flexible. The solution structure of truncated rCon-Vc11-22[Z1Q] was similar to that of the full-length peptide, indicating that the flexible C-terminus does not have any effect on the structured domain of the peptide. Contryphan-Vc1 exhibited excellent proteolytic stability against trypsin and chymotrypsin but was susceptible to pepsin digestion. We have investigated whether contryphan-Vc1 can accept a bioactive epitope while maintaining the structure of the peptide by introducing peptide sequences based on the DINNN motif of inducible nitric oxide synthase. We show that sCon-Vc11-22[NNN12-14] binds to the iNOS-binding protein SPSB2 with an affinity of 1.3 muM while maintaining the SDH fold. This study serves as a starting point in utilizing the SDH fold as a peptide scaffold.

The Single Disulfide-Directed beta-Hairpin Fold. Dynamics, Stability, and Engineering.,Chittoor B, Krishnarjuna B, Morales RAV, MacRaild CA, Sadek M, Leung EWW, Robinson SD, Pennington MW, Norton RS Biochemistry. 2017 May 16;56(19):2455-2466. doi: 10.1021/acs.biochem.7b00120., Epub 2017 May 2. PMID:28437072<ref>PMID:28437072</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5kkm" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Conus victoriae]]
[[Category: Large Structures]]
[[Category: Chittoor B]]
[[Category: Krishnarjuna B]]
[[Category: MacRaild CA]]
[[Category: Robinson SD]]