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5kkm
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Con-Vc11-22== | |
| + | <StructureSection load='5kkm' size='340' side='right' caption='[[5kkm]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5kkm]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KKM FirstGlance]. <br> | ||
| + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5kkm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kkm OCA], [http://pdbe.org/5kkm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kkm RCSB], [http://www.ebi.ac.uk/pdbsum/5kkm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kkm ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5kkm" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Chittoor, B]] | ||
| + | [[Category: Krishnarjuna, B]] | ||
| + | [[Category: MacRaild, C A]] | ||
| + | [[Category: Robinson, S D]] | ||
| + | [[Category: Contryphan-vc1]] | ||
| + | [[Category: Peptide scaffold]] | ||
| + | [[Category: Single disulfide-directed beta hairpin]] | ||
| + | [[Category: Stability]] | ||
| + | [[Category: Unknown function]] | ||
Revision as of 09:33, 27 September 2017
Con-Vc11-22
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