2o3w
From Proteopedia
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| - | [[Image:2o3w.gif|left|200px]] | ||
| - | + | ==Crystal Structure of the Homo sapiens Cytoplasmic Ribosomal Decoding Site in presence of paromomycin== | |
| - | + | <StructureSection load='2o3w' size='340' side='right'caption='[[2o3w]], [[Resolution|resolution]] 2.80Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2o3w]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O3W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O3W FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> | |
| - | - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PAR:PAROMOMYCIN'>PAR</scene></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=2o3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o3w OCA], [https://pdbe.org/2o3w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o3w RCSB], [https://www.ebi.ac.uk/pdbsum/2o3w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o3w ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | ''' | + | <div style="background-color:#fffaf0;"> |
| - | + | == Publication Abstract from PubMed == | |
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| - | == | + | |
The lack of absolute prokaryotic selectivity of natural antibiotics is widespread and is a significant clinical problem. The use of this disadvantage of aminoglycoside antibiotics for the possible treatment of human genetic diseases is extremely challenging. Here, we have used a combination of biochemical and structural analysis to compare and contrast the molecular mechanisms of action and the structure-activity relationships of a new synthetic aminoglycoside, NB33, and a structurally similar natural aminoglycoside apramycin. The data presented herein demonstrate the general molecular principles that determine the decreased selectivity of apramycin for the prokaryotic decoding site, and the increased selectivity of NB33 for the eukaryotic decoding site. These results are therefore extremely beneficial for further research on both the design of new aminoglycoside-based antibiotics with diminished deleterious effects on humans, as well as the design of new aminoglycoside-based structures that selectively target the eukaryotic ribosome. | The lack of absolute prokaryotic selectivity of natural antibiotics is widespread and is a significant clinical problem. The use of this disadvantage of aminoglycoside antibiotics for the possible treatment of human genetic diseases is extremely challenging. Here, we have used a combination of biochemical and structural analysis to compare and contrast the molecular mechanisms of action and the structure-activity relationships of a new synthetic aminoglycoside, NB33, and a structurally similar natural aminoglycoside apramycin. The data presented herein demonstrate the general molecular principles that determine the decreased selectivity of apramycin for the prokaryotic decoding site, and the increased selectivity of NB33 for the eukaryotic decoding site. These results are therefore extremely beneficial for further research on both the design of new aminoglycoside-based antibiotics with diminished deleterious effects on humans, as well as the design of new aminoglycoside-based structures that selectively target the eukaryotic ribosome. | ||
| - | + | Differential selectivity of natural and synthetic aminoglycosides towards the eukaryotic and prokaryotic decoding A sites.,Kondo J, Hainrichson M, Nudelman I, Shallom-Shezifi D, Barbieri CM, Pilch DS, Westhof E, Baasov T Chembiochem. 2007 Sep 24;8(14):1700-9. PMID:17705310<ref>PMID:17705310</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 2o3w" style="background-color:#fffaf0;"></div> |
| - | [[Category: Baasov | + | == References == |
| - | [[Category: Hainrichson | + | <references/> |
| - | [[Category: Kondo | + | __TOC__ |
| - | [[Category: Nudelman | + | </StructureSection> |
| - | [[Category: Shallom-Shezifi | + | [[Category: Large Structures]] |
| - | [[Category: Westhof | + | [[Category: Baasov T]] |
| - | + | [[Category: Hainrichson M]] | |
| - | + | [[Category: Kondo J]] | |
| - | + | [[Category: Nudelman I]] | |
| - | + | [[Category: Shallom-Shezifi D]] | |
| - | + | [[Category: Westhof E]] | |
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Current revision
Crystal Structure of the Homo sapiens Cytoplasmic Ribosomal Decoding Site in presence of paromomycin
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