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| | <StructureSection load='4ow4' size='340' side='right'caption='[[4ow4]], [[Resolution|resolution]] 2.15Å' scene=''> | | <StructureSection load='4ow4' size='340' side='right'caption='[[4ow4]], [[Resolution|resolution]] 2.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ow4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Synthetic_construct_sequences Synthetic construct sequences]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OW4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OW4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ow4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OW4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OW4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4ow4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ow4 OCA], [http://pdbe.org/4ow4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ow4 RCSB], [http://www.ebi.ac.uk/pdbsum/4ow4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ow4 ProSAT]</span></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=4ow4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ow4 OCA], [https://pdbe.org/4ow4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ow4 RCSB], [https://www.ebi.ac.uk/pdbsum/4ow4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ow4 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Synthetic construct sequences]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Blaber, M]] | + | [[Category: Blaber M]] |
| - | [[Category: Longo, L M]] | + | [[Category: Longo LM]] |
| - | [[Category: Beta-trefoil]]
| + | |
| - | [[Category: De novo]]
| + | |
| - | [[Category: De novo protein]]
| + | |
| - | [[Category: Folding nucleus symmetric expansion]]
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| - | [[Category: Protein design]]
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| - | [[Category: Top-down symmetric deconstruction]]
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| Structural highlights
Publication Abstract from PubMed
Models of symmetric protein evolution typically invoke gene duplication and fusion events, in which repetition of a structural motif generates foldable, stable symmetric protein architecture. Success of such evolutionary processes suggests that the duplicated structural motif must be capable of nucleating protein folding. If correct, symmetric expansion of a folding nucleus sequence derived from an extant symmetric fold may be an elegant and computationally tractable solution to de novo protein design. We report the efficient de novo design of a beta-trefoil protein by symmetric expansion of a beta-trefoil folding nucleus, previously identified by -value analysis. The resulting protein, having exact sequence symmetry, exhibits superior folding properties compared to its naturally evolved progenitor-with the potential for redundant folding nuclei. In principle, folding nucleus symmetric expansion can be applied to any given symmetric protein fold (that is, nearly one-third of the known proteome) provided information of the folding nucleus is available.
Evolution and design of protein structure by folding nucleus symmetric expansion.,Longo LM, Kumru OS, Middaugh CR, Blaber M Structure. 2014 Oct 7;22(10):1377-84. doi: 10.1016/j.str.2014.08.008. Epub 2014, Sep 18. PMID:25242458[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Longo LM, Kumru OS, Middaugh CR, Blaber M. Evolution and design of protein structure by folding nucleus symmetric expansion. Structure. 2014 Oct 7;22(10):1377-84. doi: 10.1016/j.str.2014.08.008. Epub 2014, Sep 18. PMID:25242458 doi:http://dx.doi.org/10.1016/j.str.2014.08.008
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