6e5i
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Heterogeneous-Backbone Mimics of a Designed Disulfide-Rich Protein: Orn turn== | |
| + | <StructureSection load='6e5i' size='340' side='right' caption='[[6e5i]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6e5i]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E5I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E5I FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DPR:D-PROLINE'>DPR</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=ORN:L-ORNITHINE'>ORN</scene></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=6e5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e5i OCA], [http://pdbe.org/6e5i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e5i RCSB], [http://www.ebi.ac.uk/pdbsum/6e5i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e5i ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Disulfide-rich peptides have found widespread use in the development of bioactive agents; however, low proteolytic stability and the difficulty of exerting synthetic control over chain topology present barriers to their application in some systems. Herein, we report a method that enables the creation of artificial backbone ("foldamer") mimics of compact, disulfide-rich tertiary folds. Systematic replacement of a subset of natural alpha-residues with various artificial building blocks in the context of a computationally designed prototype sequence leads to "heterogeneous-backbone" variants that undergo clean oxidative folding, adopt tertiary structures indistinguishable from that of the prototype, and enjoy proteolytic protection beyond that inherent to the topologically constrained scaffold. Collectively, these results demonstrate systematic backbone substitution to be a viable method to engineer the properties of disulfide-rich sequences and expands the repertoire of protein mimicry by foldamers to an exciting new structural class. | ||
| - | + | Heterogeneous-Backbone Foldamer Mimics of a Computationally Designed, Disulfide-Rich Miniprotein.,Cabalteja CC, Mihalko DS, Horne WS Chembiochem. 2019 Jan 2;20(1):103-110. doi: 10.1002/cbic.201800558. Epub 2018 Nov, 27. PMID:30326175<ref>PMID:30326175</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 6e5i" style="background-color:#fffaf0;"></div> |
| - | [[Category: Mihalko, D | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Cabalteja, C C]] | ||
| + | [[Category: Horne, W S]] | ||
| + | [[Category: Mihalko, D S]] | ||
| + | [[Category: De novo protein]] | ||
| + | [[Category: Heterogeneous backbone foldamer]] | ||
Revision as of 12:31, 16 January 2019
Heterogeneous-Backbone Mimics of a Designed Disulfide-Rich Protein: Orn turn
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