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| ==Complex of 3-alpha bound to gp41-5== | | ==Complex of 3-alpha bound to gp41-5== |
| <StructureSection load='4dzu' size='340' side='right' caption='[[4dzu]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='4dzu' size='340' side='right'caption='[[4dzu]], [[Resolution|resolution]] 2.10Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[4dzu]] 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=4DZU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DZU FirstGlance]. <br> | | <table><tr><td colspan='2'>[[4dzu]] 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=4DZU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DZU FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3o42|3o42]], [[4dzv|4dzv]]</td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=4dzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dzu OCA], [http://pdbe.org/4dzu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4dzu RCSB], [http://www.ebi.ac.uk/pdbsum/4dzu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4dzu 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=4dzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dzu OCA], [https://pdbe.org/4dzu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dzu RCSB], [https://www.ebi.ac.uk/pdbsum/4dzu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dzu ProSAT]</span></td></tr> |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| We report a new method for preorganization of alpha/beta-peptide helices, based on the use of a dense array of acidic and basic side chains. Previously we have used cyclically constrained beta residues to promote alpha/beta-peptide helicity; here we show that an engineered ion pair array can be comparably effective, as indicated by mimicry of the CHR domain of HIV protein gp41. The new design is effective in biochemical and cell-based infectivity assays; however, the resulting alpha/beta-peptide is susceptible to proteolysis. This susceptibility was addressed via introduction of a few cyclic beta residues near the cleavage site, to produce the most stable, effective alpha/beta-peptide gp41 CHR analogue identified. Crystal structures of an alpha- and alpha/beta-peptide (each involved in a gp41-mimetic helix bundle) that contain the dense acid/base residue array manifest disorder in the ionic side chains, but there is little side-chain disorder in analogous alpha- and alpha/beta-peptide structures with a sparser ionic side-chain array. These observations suggest that dense arrays of complementary acidic and basic residues can provide conformational stabilization via Coulombic attractions that do not require entropically costly ordering of side chains.
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| Enhancement of alpha-Helix Mimicry by an alpha/beta-Peptide Foldamer via Incorporation of a Dense Ionic Side-Chain Array.,Johnson LM, Mortenson DE, Yun HG, Horne WS, Ketas TJ, Lu M, Moore JP, Gellman SH J Am Chem Soc. 2012 Apr 23. PMID:22524614<ref>PMID:22524614</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 4dzu" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Gp41|Gp41]] | | *[[Gp41 3D Structures|Gp41 3D Structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Synthetic construct sequences]] | | [[Category: Large Structures]] |
| [[Category: Gellman, S H]] | | [[Category: Synthetic construct]] |
| [[Category: Horne, W S]] | | [[Category: Gellman SH]] |
| [[Category: Johnson, L M]] | | [[Category: Horne WS]] |
| [[Category: Ketas, T J]] | | [[Category: Johnson LM]] |
| [[Category: Lu, M]] | | [[Category: Ketas TJ]] |
| [[Category: Moore, J P]] | | [[Category: Lu M]] |
| [[Category: Mortenson, D E]] | | [[Category: Moore JP]] |
| [[Category: Yun, H G]] | | [[Category: Mortenson DE]] |
| [[Category: De novo protein]]
| | [[Category: Yun HG]] |
| [[Category: Viral fusion]]
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