2tbd
From Proteopedia
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| - | [[Image:2tbd.jpg|left|200px]]<br /><applet load="2tbd" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2tbd" /> | ||
| - | '''SV40 T ANTIGEN DNA-BINDING DOMAIN, NMR, 30 STRUCTURES'''<br /> | ||
| - | == | + | ==SV40 T ANTIGEN DNA-BINDING DOMAIN, NMR, 30 STRUCTURES== |
| + | <StructureSection load='2tbd' size='340' side='right'caption='[[2tbd]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2tbd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Macaca_mulatta_polyomavirus_1 Macaca mulatta polyomavirus 1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2TBD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2TBD 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2tbd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2tbd OCA], [https://pdbe.org/2tbd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2tbd RCSB], [https://www.ebi.ac.uk/pdbsum/2tbd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2tbd ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q98ZP7_SV40 Q98ZP7_SV40] | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tb/2tbd_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2tbd ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The structure of the domain from simian virus 40 (SV40) large T-antigen that binds to the SV40 origin of DNA replication (T-ag-OBD131-260) has been determined by nuclear magnetic resonance spectroscopy. The overall fold, consisting of a central five-stranded antiparallel beta-sheet flanked by two alpha-helices on one side and one alpha-helix and one 3(10)-helix on the other, is a new one. Previous mutational analyses have identified two elements, termed A (approximately 152-155) and B2 (203-207), as essential for origin-specific recognition. These elements form two closely juxtaposed loops that define a continuous surface on the protein. The addition of a duplex oligonucleotide containing the origin recognition pentanucleotide GAGGC induces chemical shift changes and slows amide proton exchange in resonances from this region, indicating that this surface directly contacts the DNA. | The structure of the domain from simian virus 40 (SV40) large T-antigen that binds to the SV40 origin of DNA replication (T-ag-OBD131-260) has been determined by nuclear magnetic resonance spectroscopy. The overall fold, consisting of a central five-stranded antiparallel beta-sheet flanked by two alpha-helices on one side and one alpha-helix and one 3(10)-helix on the other, is a new one. Previous mutational analyses have identified two elements, termed A (approximately 152-155) and B2 (203-207), as essential for origin-specific recognition. These elements form two closely juxtaposed loops that define a continuous surface on the protein. The addition of a duplex oligonucleotide containing the origin recognition pentanucleotide GAGGC induces chemical shift changes and slows amide proton exchange in resonances from this region, indicating that this surface directly contacts the DNA. | ||
| - | + | Solution structure of the origin DNA-binding domain of SV40 T-antigen.,Luo X, Sanford DG, Bullock PA, Bachovchin WW Nat Struct Biol. 1996 Dec;3(12):1034-9. PMID:8946857<ref>PMID:8946857</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2tbd" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Large T Antigen|Large T Antigen]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Macaca mulatta polyomavirus 1]] | ||
| + | [[Category: Bachovchin WW]] | ||
| + | [[Category: Bullock PA]] | ||
| + | [[Category: Luo X]] | ||
| + | [[Category: Sanford DG]] | ||
Current revision
SV40 T ANTIGEN DNA-BINDING DOMAIN, NMR, 30 STRUCTURES
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