8if5
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 8if5 is ON HOLD Authors: Xu, G.H., Wang, C., Li, C.G. Description: AFB1-AF26 APTAMER COMPLEX Category: Unreleased Structures [[Category: Li, C....) |
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| - | '''Unreleased structure''' | ||
| - | + | ==AFB1-AF26 APTAMER COMPLEX== | |
| + | <StructureSection load='8if5' size='340' side='right'caption='[[8if5]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8if5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8IF5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8IF5 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AFT:AFLATOXIN+B1'>AFT</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=8if5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8if5 OCA], [https://pdbe.org/8if5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8if5 RCSB], [https://www.ebi.ac.uk/pdbsum/8if5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8if5 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The 26-mer DNA aptamer (AF26) that specifically binds aflatoxin B1 (AFB1) with nM-level high affinity is rare among hundreds of aptamers for small molecules. Despite its predicted stem-loop structure, the molecular basis of its high-affinity recognition of AFB1 remains unknown. Here, we present the first high-resolution nuclear magnetic resonance structure of AFB1-AF26 aptamer complex in solution. AFB1 binds to the 16-residue loop region of the aptamer, inducing it to fold into a compact structure through the assembly of two bulges and one hairpin structure. AFB1 is tightly enclosed within a cavity formed by the bulges and hairpin, held in a place between the G.C base pair, G.G.C triple and multiple T bases, mainly through strong pi-pi stacking, hydrophobic and donor atom-pi interactions, respectively. We further revealed the mechanism of the aptamer in recognizing AFB1 and its analogue AFG1 with only one-atom difference and introduced a single base mutation at the binding site of the aptamer to increase the discrimination between AFB1 and AFG1 based on the structural insights. This research provides an important structural basis for understanding high-affinity recognition of the aptamer, and for further aptamer engineering, modification and applications. | ||
| - | + | Structural basis for high-affinity recognition of aflatoxin B1 by a DNA aptamer.,Xu G, Wang C, Yu H, Li Y, Zhao Q, Zhou X, Li C, Liu M Nucleic Acids Res. 2023 Jun 23:gkad541. doi: 10.1093/nar/gkad541. PMID:37351632<ref>PMID:37351632</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Li | + | <div class="pdbe-citations 8if5" style="background-color:#fffaf0;"></div> |
| - | [[Category: Wang | + | == References == |
| - | [[Category: Xu | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Synthetic construct]] | ||
| + | [[Category: Li CG]] | ||
| + | [[Category: Wang C]] | ||
| + | [[Category: Xu GH]] | ||
Current revision
AFB1-AF26 APTAMER COMPLEX
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