5jlx
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==AntpHD with 15bp DNA duplex S-monothiolated at Cytidine-8== | |
+ | <StructureSection load='5jlx' size='340' side='right' caption='[[5jlx]], [[Resolution|resolution]] 2.75Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[5jlx]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JLX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JLX FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr> | ||
+ | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=C7S:2-DEOXY-5-O-THIOPHOSPHONOCYTIDINE'>C7S</scene></td></tr> | ||
+ | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5jlw|5jlw]]</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=5jlx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jlx OCA], [http://pdbe.org/5jlx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jlx RCSB], [http://www.ebi.ac.uk/pdbsum/5jlx PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/ANTP_DROME ANTP_DROME]] Sequence-specific transcription factor which is part of a developmental regulatory system that regulates segmental identity in the mesothorax. Provides cells with specific positional identities on the anterior-posterior axis. | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Oxygen-to-sulfur substitutions in DNA phosphate often enhance affinity for DNA-binding proteins. Our previous studies have suggested that this effect of sulfur substitution of both OP1 and OP2 atoms is due to an entropic gain associated with enhanced ion-pair dynamics. In this work, we studied stereospecific effects of single sulfur substitution of either the OP1 or OP2 atom in DNA phosphate at the Lys57 interaction site of the Antennapedia homeodomain-DNA complex. By crystallography, we obtained the structural information on the RP and SP diastereomers of the phosphoromonothioate and their interaction with Lys57. By fluorescence-based assays, we found significant affinity enhancement upon sulfur substitution of the OP2 atom. By NMR spectroscopy, we found significant mobilization of the Lys57 side-chain NH3+ group upon sulfur substitution of the OP2 atom. These data provide further mechanistic insight into the affinity enhancement by oxygen-to-sulfur substitution in DNA phosphate. | ||
- | + | Stereospecific effects of oxygen-to-sulfur substitution in DNA phosphate on ion-pair dynamics and protein-DNA affinity.,Nguyen D, Zandarashvili L, White MA, Iwahara J Chembiochem. 2016 Jun 7. doi: 10.1002/cbic.201600265. PMID:27271797<ref>PMID:27271797</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
+ | <div class="pdbe-citations 5jlx" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Iwahara, J]] | ||
+ | [[Category: Nguyen, D]] | ||
+ | [[Category: White, M A]] | ||
+ | [[Category: Zandarashvili, L]] | ||
+ | [[Category: Dna-binding protein]] | ||
+ | [[Category: Homeodomain]] | ||
+ | [[Category: Monothiolated dna]] | ||
+ | [[Category: Transcription regulator-dna complex]] | ||
+ | [[Category: Transcription-dna complex]] |
Revision as of 23:11, 23 June 2016
AntpHD with 15bp DNA duplex S-monothiolated at Cytidine-8
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